ライフサイエンスコーパス: FKBP

1 FKBP family members are targets for drugs such as rapamy

2 FKBP gene expression coordinately induces the expression

3 FKBP-domain proteins (FKBPs) are pivotal modulators of c

4 t of rapamycin and FK506-binding protein 12 (FKBP), respectively, the optimized FRB-N-terminal lucife

5 ELP nanoparticles, FK506 binding protein 12 (FKBP), which is the cognate protein target of Rapa, was

6 athrin by using an FK506-binding protein 12 (FKBP)-clathrin fusion protein that is specifically oligo

7 membrane-bound, adipocyte-specific caspase 8-FKBP fusion protein.

8 The slyD gene encodes a FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase).

9 e show here that induced dimerization of Abl-FKBP, but not the kinase-defective AblKD-FKBP, inhibits

10 Abl-FKBP, but not the kinase-defective AblKD-FKBP, inhibits cell spreading on fibronectin.

11 Activation of this nuclear AblNuk-FKBP by dimerization with AP20187 in anaplastic thyroid

12 as in its closed state or when applied after FKBP binding had occurred, whereas diamide was always ef

13 A second major conformation of apo AIPL1-FKBP was identified by NMR studies.

14 e solved the crystal structures of the AIPL1-FKBP domain and its pathogenic mutant V71F, both in the

15 We find that although FKBP-ERGIC-53 of the ER-Golgi intermediate compartment (

16 This procedure involves coexpressing an FKBP-tagged Golgi enzyme with an ER-retained protein fus

17 FRAP (FKBP-rapamycin-associated protein), an FKBP-tagged Golgi enzyme can be trapped when it visits t

18 FKBP12-tagged Golgi enzyme for binding to an FKBP-rapamycin binding domain (FRB)-tagged ER trap.

19 rin-coated vesicles (CCVs), together with an FKBP and rapamycin-binding domain-containing construct w

20 hat is recognized by the cyclophilin-CsA and FKBP-FK506 complexes.

21 , cyclophilin A-cyclosporin A (CyPA-CsA) and FKBP-FK506.

22 mily immunophilins that contain both CyP and FKBP domains for which we propose the name FCBP (FK506-

23 e) were also identified in which the CyP and FKBP domains were in the reverse order.

24 D, Tmp-SLF, which dimerizes E. coli DHFR and FKBP and has no endogenous mammalian targets that would

25 rotein-protein interactions between DHFR and FKBP preclude formation of a trimeric complex.

26 A combined model of the RyR fragment and FKBP docked into the cryo-EM map suggests that the fragm

27 mycin in samples overexpressing both FRB and FKBP (FRB.rapamycin+FKBP, Kd approximately 100 fM; FKBP.

28 ion of these domains to the proteins FRB and FKBP enabled their induced assembly by the natural produ

29 e different proteins, calmodulin, NmerA, and FKBP, shows that selective labeling with [(13)C]methyl g

30 The rapamycin and FKBP-target 1 (RAFT1), also known as FKBP12-rapamycin-as

31 Evidence for an interaction between RyR and FKBP is well documented, both in skeletal muscle (RyR1-F

32 All 12 cyclophilins and FKBPs are dispensable for growth in yeast, whereas the o

33 owed that controlled homodimerization of APP-FKBP leads to a 50% reduction in total Abeta levels in t

34 P20187 induces rapid dimerization of the APP-FKBP chimera.

35 FKBP(*), but Q53D unfolded twice as fast as FKBP(*).

36 apamycin-binding proteins are abbreviated as FKBPs.

37 hat the chromatin binding ability of 'basic' FKBPs is shared amongst related orthologues present in f

38 n, which induces a tight association between FKBP (FK506-binding protein) and FRAP (FKBP-rapamycin-as

39 apamycin induces a tight association between FKBP and FRAP, one would expect rapamycin to trap the FK

40 The rapamycin-controlled interaction between FKBP and FRB proteins could be detected in vitro and in

41 No interaction between FKBP and FRB was detected in the absence of rapamycin.

42 horough analysis of the interactions between FKBP, rapamycin, and the rapamycin-binding domain of mTO

43 1903, a bivalent "dimerizer" drug that binds FKBP and induces Fas cross-linking.

44 ng to be initiated by addition of a bivalent FKBP ligand.

45 Both FKBPs and CYPs can be classified into single domain and

46 prevented the formation of BiFC complexes by FKBP and FRB fusions, but did not disrupt existing BiFC

47 asive and antimetastatic effects produced by FKBP gene expression.

48 This canonical FKBP domain actively increases the rate of isomerization

49 both a 50-residue insertion in the catalytic FKBP domain, also called 'Insert-in-Flap' or IF domain,

50 lathrin function with a clathrin light chain-FKBP chimera oligomerizable by the drug AP20187.

51 on this basis are divided into two classes: FKBPs bind to FK506 and rapamycin, while cyclophilins bi

52 (NLuc)/C-terminal luciferase fragment (CLuc)-FKBP luciferase complementation imaging (LCI) pair recon

53 plants of cells expressing the FRB-NLuc/CLuc-FKBP LCI pair, dose- and time-dependent luciferase activ

54 s validated on two protein-ligand complexes: FKBP complexed to 2-(3'-pyridyl)-benzimidazole and MurA

55 s composed of three domains: two consecutive FKBP domains and a three-unit repeat of the TPR (tetratr

56 This is because ER-Golgi-cycling FKBP proteins contain a C-terminal KDEL-like sequence, b

57 nants using FRET, we created five single-Cys FKBP variants labeled with Alexa Fluor 488 (denoted D-FK

58 ants labeled with Alexa Fluor 488 (denoted D-FKBP) and then targeted these D-FKBPs to full-length RyR

59 stance analysis of FRET measured from each D-FKBP variant to Cy3NTA bound to each His tag.

60 Results indicate that D-FKBP binds proximal to both N-terminal and central domai

61 8 (denoted D-FKBP) and then targeted these D-FKBPs to full-length RyR1 constructs containing decahist

62 gulatable protein destabilization domain (dd-FKBP).

63 supporting a novel hypothesis that declining FKBP function plays a major role in unhealthy brain agin

64 monstrated that oxidizing reagents decreased FKBP binding.

65 BPs covering ten of the twenty-two different FKBP domains.

66 ) fusion protein was stimulated by a dimeric FKBP ligand.

67 localized AtCYP57, and one nucleus directed FKBP known as AtFKBP65.

68 osase with ERT2 and two degradation domains (FKBP-DD, DHFR-DD), in multiple orientations, and determi

69 K), AKT (protein kinase B), and its effector FKBP-rapamycin-associated protein (FRAP) occurs via auto

70 a critical role for Hsp90 binding by either FKBP.

71 Of the many eukaryotic FKBPs that have been identified, FKBP65 is an endoplasmi

72 This mutant (F36V-FKBP) is capable of binding, with low or subnanomolar af

73 The complexes of CsA-CyP and of FK506-FKBP both bind to and inhibit the activity of the calciu

74 Assessment of fluorescent FKBP binding in myocyte revealed a high FKBP12.6-RyR2 af

75 Each of the five fluorescent FKBPs retained the ability to inhibit [(3)H]ryanodine bi

76 FRB.rapamycin+FKBP, Kd approximately 100 fM; FKBP.rapamycin+FRB, Kd = 12 nM).

77 we show that the best potential binders for FKBP proteins optimally expose the two contiguous carbon

78 onyl oxygen in the proline-mimetic chain for FKBP docking and are characterized by the abundance of r

79 bic cluster within SPRY1 that is crucial for FKBP binding.

80 As one of four FKBPs within the yeast Saccharomyces cerevisiae, Fpr4 ha

81 istone prolyl isomerase activities, the Fpr4 FKBP domain binds to nucleosomes and nucleosome arrays i

82 The interaction of the Fpr4 FKBP with recombinant chromatin complexes condenses nucl

83 tween FKBP (FK506-binding protein) and FRAP (FKBP-rapamycin-associated protein), an FKBP-tagged Golgi

84 n kinase B), and the downstream kinase FRAP (FKBP-rapamycin-associated protein).

85 on of FKBP (FK-506 binding protein) and FRB (FKBP-rapamycin binding protein) upon UV irradiation.

86 eta produces GSK-3beta fused to a tag, FRB* (FKBP/rapamycin binding), resulting in a rapidly destabil

87 tein-protein interactions can be imaged (FRB-FKBP, Fos-Jun, and neuroligin-PSD-95), with as little as

88 Using a model receptor-ligand pair (FRB-FKBP), we first test physical and computational predicti

89 phosphatase module through the rapamycin/FRB/FKBP system or by treatment with ionomycin.

90 a inhibitor GRK2ct (GRK2ct-KERE) and the FRB/FKBP heterodimerization system.

91 e FKBP12-rapamycin-binding (FRB) domain from FKBP-12-rapamycin associated protein 1 (FRAP1, also know

92 activity, indicating that it is a functional FKBP.

93 We made a calpain-GFP-FKBP fusion through single cross-over integration at the

94 lial cells stably expressing a chimeric HER2-FKBP molecule that could be conditionally induced to hom

95 duced growth of MCF10A cells expressing HER2-FKBP.

96 21 (43%) genes overexpressed by HGA were HIF/FKBP-associated genes.

97 sequence and structural comparison of human FKBP domains.

98 ficacy is decreased in the presence of human FKBP due to the high concentration of FKBP and its tight

99 urse of protein engineering studies on human FKBP, we discovered that a single point mutation in the

100 ta are available for eight of fourteen human FKBPs covering ten of the twenty-two different FKBP doma

101 mycin that also express invariant chain (Ii)-FKBP in the ER.

102 ST-FRB is trapped in the ER even without Ii-FKBP upon rapamycin addition.

103 when added to cells expressing an alpha(IIb)(FKBP)(2) chimera complexed with beta(3).

104 mutation, N760D, appears to directly impact FKBP binding through interfering with SPRY1 folding.

105 in the urea-unfolded state that were not in FKBP(*), indicating that the mutations had a more substa

106 hibits mTOR function by interacting with its FKBP-rapamycin-binding (FRB) domain.

107 Clustering of GP Ib-IX(FKBP)(2) also stimulated rapid tyrosine phosphorylation

108 tail to tandem repeats of FKBP, and GP Ib-IX(FKBP)(2) and alpha(IIb)beta(3) were expressed in Chinese

109 Moreover, clustering of GP Ib-IX(FKBP)(2) by AP20187 led to an increase in alpha(IIb)beta

110 Conditional oligomerization of GP Ib-IX(FKBP)(2) by AP20187, a cell-permeable FKBP dimerizer, ca

111 ll shear rates of up to 2000 s(-1), GP Ib-IX(FKBP)(2) mediated cell tethering to immobilized VWF, jus

112 FKBP51 (the 51-kDa FKBP) associates with heat shock protein 90 (Hsp90) and

113 eptor-labeled CaM binding near donor-labeled FKBP (FK506-binding protein 12.6) on the cytoplasmic dom

114 ponses via isomerase-independent mechanisms, FKBPs are most highly expressed in the nervous system, w

115 GIC) rapidly cycles through the ER (30 min), FKBP-Golgi enzyme chimeras remain stably associated with

116 horylation within 1 min, whereas a monomeric FKBP ligand had no effect.

117 natural products, which tightly bind to most FKBP family members, including FKBP51 and FKBP52.

118 o (c4F2) copies of the AP1510 binding motif (FKBP) transformed NIH 3T3 cells in a ligand-dependent ma

119 This structure of a multi-FKBP domain protein clarifies the arrangement of these d

120 ne the pharmacological relevance of multiple FKBP members in the immunosuppressant-induced T-cell ina

121 cking the macrolide structure of the natural FKBP binders FK506 and Rapamycin.

122 RyR2 channel complex, did not restore normal FKBP binding under oxidizing conditions.

123 and by extension to mTOR, in the absence of FKBP is of little consequence under physiological condit

124 these findings, we propose that addition of FKBP-binding groups might partially overcome the poor ph

125 To investigate the structural basis of FKBP interactions with the RyR1 and RyR2 isoforms, we us

126 human FKBP due to the high concentration of FKBP and its tight affinity for MTXSLF.

127 cin derivative induced rapid dimerization of FKBP (FK-506 binding protein) and FRB (FKBP-rapamycin bi

128 d in other systems where the dimerization of FKBP has been used to initiate signaling pathways, offer

129 cation of chemically induced dimerization of FKBP to create nearly instantaneous high-affinity bivale

130 on domain to the rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP).

131 their delivery was impaired by expression of FKBP-clathrin chimeras and AP20187 incubation.

132 ng as a gatekeeper residue in the folding of FKBP(*).

133 The AP20187-induced dimeric form of FKBP-Cdc34 was substantially more active than the monome

134 The fusion of FKBP to these nanoparticles slowed the terminal half-lif

135 e showed that Shld1, the chemical inducer of FKBP-DD, does not interfere with stem cell differentiati

136 Treatment with the FK506 inhibitor of FKBP-FRB interaction prevented the formation of BiFC com

137 These findings show the involvement of FKBP proteins at different stages of PrP(C) biogenesis a

138 of mechanistic interest within FRET range of FKBP.

139 at its cytoplasmic tail to tandem repeats of FKBP, and GP Ib-IX(FKBP)(2) and alpha(IIb)beta(3) were e

140 Thus, a subclass of FKBP prolyl isomerase enzymes is recruited to linker reg

141 tes of Q53N and Q53T were similar to that of FKBP(*), but Q53D unfolded twice as fast as FKBP(*).

142 etic folding intermediate similar to that of FKBP(*).

143 s in Arabidopsis is that a large fraction of FKBPs and CYPs are localized in the chloroplast, a possi

144 FKBP12 is the only FKBP family member that plays a key role in immunosuppre

145 , perhaps, specific targets of either CyP or FKBP inhibitable by one drug alone.

146 6- and rapamycin-binding protein (FKBP12, or FKBP) and the FKBP-rapamycin binding (FRB) domain of the

147 ntly in samples overexpressing either FRB or FKBP alone (rapamycin+FKBP, Kd approximately 0.2 nM; rap

148 n of DNA sequences encoding FRB+rapamycin or FKBP+rapamycin in samples overexpressing both FRB and FK

149 Unlike any other FKBP characterized so far, FKBP65 is developmentally reg

150 PIase domains differs from that of the other FKBP family members.

151 Other FKBPs, especially the larger ones, participate in import

152 ugh FKBP51 shares characteristics with other FKBPs, it also has unique features, especially the role

153 ase in both adherence and spreading of PECAM/FKBP-2-transfected cells on immobilized fibronectin, a r

154 Ib-IX(FKBP)(2) by AP20187, a cell-permeable FKBP dimerizer, caused a decrease in cell translocation

155 addition of the bivalent, membrane-permeable FKBP dimerizer, AP1510, nearly doubled homophilic bindin

156 ncentration of the weaker binding Plasmodium FKBP has no effect on the inhibitory potency of MTXSLF i

157 the complex of FK506 and its binding protein FKBP also binds.

158 ovalently linked to a ligand for the protein FKBP to create a bifunctional molecule called MTXSLF.

159 h-level expression of FK506-binding protein (FKBP) 12 by HGA.

160 ytes deficient in the FK506-binding protein (FKBP) 12, a target of rapamycin activity, had reduced pr

161 fusion protein of the FK506 binding protein (FKBP) and caspase 8 under control of the albumin promote

162 teraction between the FK506 binding protein (FKBP) and the FKBP-rapamycin binding domain (FRB).

163 y relies on a mutated FK506-binding protein (FKBP) destabilizing domain (dd) fused to the protein of

164 Typically, FK506-binding protein (FKBP) domains are fused to a signaling domain of interes

165 containing one or two FK506-binding protein (FKBP) domains at their COOH terminus.

166 The FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases (PPIases) is

167 The FK506 binding protein (FKBP) family of proteins provide an interesting series o

168 BP38, a member of the FK506-binding protein (FKBP) family that is structurally related to FKBP12.

169 Mips are part of the FK506-binding protein (FKBP) family, whose members typically exhibit peptidylpr

170 constructed an AblNuk-FK506-binding protein (FKBP) fusion protein to enforce the nuclear accumulation

171 ion of a TRH receptor-FK506-binding protein (FKBP) fusion protein was stimulated by a dimeric FKBP li

172 cule used to dimerize FK506-binding protein (FKBP) fusion proteins and initiate biological signaling

173 incorporated into an FK506 binding protein (FKBP) fusion to allow for its specific activation using

174 erized member of the FK-506-binding protein (FKBP) gene family down-regulated in aggressive tumors.

175 The FK506-binding protein (FKBP) is an important regulator of channel activity, and

176 teine variants of the FK506-binding protein (FKBP) labeled with a donor probe, and DPc10 labeled with

177 l-permeable, bivalent FK506-binding protein (FKBP) ligand stimulated clustering when added to cells e

178 e dimerization domain FK506-binding protein (FKBP) or to the hexameric protein CcmK4 from cyanobacter

179 20-2, belongs to the FK-506 binding protein (FKBP) subfamily that functions as peptidyl-prolyl isomer

180 se 9 fused to a human FK506 binding protein (FKBP) to allow conditional dimerization using a small mo

181 using a domain of the FK506-binding protein (FKBP) to the C terminus of APP.

182 thermore, fusion of a FK506-binding protein (FKBP) to the N terminus of human Cdc34 yielded FKBP-Cdc3

183 d by interaction with FK506-binding protein (FKBP), and disruption of the RyR-FKBP association has be

184 es with a fluorescent FK506-binding protein (FKBP), and FRET was determined following incubations in

185 cyclophilin (CyP) and FK506-binding protein (FKBP), respectively.

186 Expression of FK506 binding protein (FKBP)-clathrin light chain chimeras, to inhibit clathrin

187 tures two independent FK506-binding protein (FKBP)-like and tetratricopeptide repeat domains.

188 evealed that both the FK506 binding protein (FKBP)-like domain and the tetratricopeptide repeat (TPR)

189 The rapamycin and FK506-binding protein (FKBP)-target 1 (RAFT1, also known as FRAP) is a mammalia

190 ytoplasmic chaperone, FK506-binding protein (FKBP).

191 n, and 2 copies of an FK506-binding protein (FKBP).

192 in is located next to FK506-binding protein (FKBP).

193 nts involving RyR and FK506-binding protein (FKBP).

194 associated with the FK506 binding proteins (FKBP) -52 and -51 response to cortisol exposure in neuro

195 The FK506-binding proteins (FKBP) 51 and 52 are cochaperones that modulate the signa

196 FK506-binding proteins (FKBP) 51 and 52 are cochaperones that modulate the signa

197 FK506-binding proteins (FKBP) are immunophilins that interact with the immunosup

198 ified: cyclophilins, FK506-binding proteins (FKBPs) and parvulins.

199 FK506-binding proteins (FKBPs) are cellular receptors for immunosuppressants tha

200 FK506-binding proteins (FKBPs) are peptidyl-prolyl cis/trans isomerases PPIases)

201 similarity to human FK506-binding proteins (FKBPs) in residues 166 to 252 located in the globular do

202 FK506-binding proteins (FKBPs) represent one of the three families of enzymes sh

203 nophilins, including FK506-binding proteins (FKBPs), are protein chaperones with peptidyl-prolyl isom

204 amily comprising the FK506-binding proteins (FKBPs), cyclophilins, and parvulins.

205 ressive ligands for FK-506 binding proteins (FKBPs).

206 ilins (CyPs) and the FK506-binding proteins (FKBPs).

207 ly of immunophilins, FK506 binding proteins (FKBPs).

208 include calstabins [FK506-binding proteins (FKBPs)], calmodulin (CaM), phosphodiesterase, kinases, p

209 FKBP-domain proteins (FKBPs) are pivotal modulators of cellular signaling, pro

210 nd simultaneously to two different proteins, FKBP and mTOR.

211 ns in the first LP dipeptide in the putative FKBP binding domain eliminated FKBP12 and FKBP52 interac

212 bond from Tyr(113) that mimics the putative FKBP transition state.

213 e immunophilins, among which 23 are putative FKBPs and 29 are putative CYPs.

214 pressing either FRB or FKBP alone (rapamycin+FKBP, Kd approximately 0.2 nM; rapamcyin+FRB, Kd = 26 mu

215 rexpressing both FRB and FKBP (FRB.rapamycin+FKBP, Kd approximately 100 fM; FKBP.rapamycin+FRB, Kd =

216 orylation, and is inhibited by the Rapamycin/FKBP-12 complex.

217 colocalizes with endogenous and recombinant FKBP chimeric clathrin polypeptides in PC12-cell endosom

218 ite biology, we adapted a ligand-regulatable FKBP protein destabilization domain (ddFKBP) for use in

219 ere stably transfected with siRNA-resistant, FKBP-tagged subunits of the adaptor protein (AP) complex

220 ng protein (FKBP), and disruption of the RyR-FKBP association has been implicated in cardiomyopathy,

221 esent study, we investigated whether the RyR-FKBP association is redox-regulated.

222 Several FKBP family members such as FKBP12, FKBP12.6, and FKBP51

223 cted parasites could be modulated by a small FKBP ligand, Shield1 (Shld1).

224 Some FKBPs, notably FKBP12 (the 12-kDa FK506-binding protein)

225 ursor of beta-secretase cleavage, C99/SPA4CT-FKBP.

226 thin sections of fly heads revealed specific FKBP immunoreactivity associated with the eye.

227 that the protein heterodimerization switches FKBP-rapalog-FRB can be harnessed in engineered COS-7 ce

228 for its specific activation using synthetic FKBP ligands.

229 eoplasmin-like (NPL) domain and a C-terminal FKBP peptidyl-proline isomerase domain.

230 , a protozoan parasite, contained N-terminal FKBP and C-terminal CyP domains joined by tetratricopept

231 Although the N-terminal FKBP-like domain of AIPL1 binds the farnesylated PDE6alp

232 e additional residues at the amino terminus (FKBP(*)).

233 D and Q53T mutants also refolded faster than FKBP(*) but lacked the folding intermediate, indicating

234 folding trajectory and transition state than FKBP(*) and Q53N.

235 The FKBP and FRB domains, which are dimerized by rapamycin a

236 The FKBP-12-rapamycin associated protein (FRAP, also known a

237 onally induced to homodimerize by adding the FKBP ligand AP1510, or instead induced to heterodimerize

238 eening a small dipeptide library against the FKBP-FRB protein complex involved in cell cycle arrest.

239 strained by both the RyR cryo-EM map and the FKBP atomic structure docked to the RyR.

240 ionship between histone deacetylases and the FKBP enzymes and provide a novel and critical function f

241 in-binding protein (FKBP12, or FKBP) and the FKBP-rapamycin binding (FRB) domain of the mammalian tar

242 een the FK506 binding protein (FKBP) and the FKBP-rapamycin binding domain (FRB).

243 at the HD2-type histone deacetylases and the FKBP-type PPIases may have evolved from a common ancesto

244 We believe the FKBP-based PB transposon induction will be useful for tr

245 inities of two protein-ligand complexes: the FKBP protein bound with small molecules 4-hydroxy-2-buta

246 We have generated docking poses for the FKBP-GPI complex using eight docking programs, and compa

247 ins, and the FK506-binding proteins form the FKBP subfamily of immunophilins.

248 eptidyl-prolyl-isomerase (PPI) function, the FKBP protein family is at the crossroad of several impor

249 X compound and the minimal pharmacore in the FKBP family, shedding new light on the isomerization mec

250 lter phoshorylation of receptors lacking the FKBP domain.

251 domain elements are closely apposed near the FKBP binding site within the RyR1 three-dimensional stru

252 ther Mn or a self-interacting version of the FKBP domain.

253 Recently FK506, an inhibitor of the FKBP family of peptidyl prolyl isomerases, was shown to

254 hat dimerization is a latent property of the FKBP fold: the crystal structure reveals a remarkably co

255 of the FKBP65 gene and other members of the FKBP multigene family were therefore investigated from a

256 ike 1 (AIPL1) is a distinctive member of the FKBP superfamily in terms of its biochemical properties,

257 e (RyR2-FKBP12.6), however definition of the FKBP-binding site remains elusive.

258 affinities involved in the formation of the FKBP.rapamycin.FRB complex, we used fluorescence polariz

259 cesses that do not necessarily depend on the FKBP domain.

260 (SAR) of small molecules that mimic only the FKBP binding domain portion of FK506 has focused on este

261 l and pipecolyl esters, which mimic only the FKBP binding domain portion of FK506, are proposed and a

262 ogical inhibitors of the PI 3'-kinase or the FKBP 12-rapamycin-associated protein/mammalian target of

263 rotein (FKBP12, also known as FKBP1A) or the FKBP-rapamycin binding (FRB) domain of the mammalian tar

264 al domains of RyR1, thus suggesting that the FKBP binding site is composed of determinants from both

265 These analyses suggest that the FKBP multigene family emerged early in the evolutionary

266 We found that the FKBP-DD confers the PB transposase with a higher transpo

267 In addition, we found that the FKBP-DD regulates transposon activity in a reversible an

268 Binding of FK506 to the FKBP domain causes the target domain to first unfold, th

269 e binding of isoprenyl groups on PDE6 to the FKBP domain of AIPL1.

270 nd have a C-terminal domain belonging to the FKBP fold.

271 t the fragment is positioned adjacent to the FKBP-binding site.

272 binding of the farnesylated-Cys probe to the FKBP-like domain of AIPL1, thus uncovering a novel funct

273 FRAP, one would expect rapamycin to trap the FKBP-fused Golgi protein in the ER if it ever visits the

274 nsight into its biological role, we used the FKBP degradation domain system to generate a fusion prot

275 nrelated Golgi-targeted constructs using the FKBP strategy.

276 ipid binding that is unparalleled within the FKBP superfamily.

277 rovide a novel and critical function for the FKBPs.

278 e structural and functional diversity of the FKBPs.

279 It has been speculated that these FKBPs are possibly redundant in the immunosuppressant-in

280 lit-tyrosine phosphatases (PTPs) attached to FKBP and FRB, where catalytic activity can be modulated

281 hus ST-FRB cycles artificially by binding to FKBP domain-containing proteins.

282 ular component of whole blood via binding to FKBP.

283 s split into two moieties that were fused to FKBP (FK506-binding protein) and FRB (rapamycin-binding

284 ments of yellow fluorescent protein fused to FKBP and FRB produced detectable BiFC complex fluorescen

285 nt of the Venus fluorescent protein fused to FKBP produced constitutive BiFC complexes with several C

286 s the Q53N mutant was stabilized relative to FKBP(*) with little change in the equilibrium m values.

287 The two FKBP domains differ by an insertion in the second that a

288 shows decreased CaM affinity, but unaltered FKBP 12.6 affinity.

289 vestigate the molecular basis of this unique FKBP-dependence, spontaneous plaque-forming mutants of p

290 Unlike FKBP-FK506, CyPA-CsA interacts with Arg-122 at the activ

291 he affinities of the inducers for unmodified FKBP and FRB.

292 c myocyte environment can be monitored using FKBP biosensors and FRET.

293 These receptor heterocomplexes contain wheat FKBPs, and they bind rabbit cytoplasmic dynein in a PPIa

294 CPS was still triggered by rapamycin when FKBP and FRB occupied one or both of the extein position

295 To test whether FKBP interaction determined localization, we overexpress

296 The comparison of CyPA-CsA-CN with FKBP-FK506-CN significantly contributes to understanding

297 tate of the RyR is intimately connected with FKBP binding affinity.

298 Its predicted binding interface with FKBP consists primarily of electrostatic contacts and co

299 The interaction with FKBPs was found to be surprisingly tolerant to the stere

300 BP) to the N terminus of human Cdc34 yielded FKBP-Cdc34 that was induced to form a dimer upon treatme