ライフサイエンスコーパス: protomer

1 e with a single transmembrane domain in each protomer.

2 s bound to both the D1 and D2 domains of the protomer.

3 ing that incorporation requires a Spr28-Spr3 protomer.

4 odulate the binding of dopamine at the other protomer.

5 ion and approximately 5,000 residues in each protomer.

6 ccess and deep drug binding pockets in every protomer.

7 aining at least 26 transmembrane helices per protomer.

8 inhibit the binding of dopamine at the other protomer.

9 three different conformations of the active protomer.

10 operativity in hydrolysis of the ATP in each protomer.

11 acellular ends of TM2 and TM7 within the D2R protomer.

12 47 in transmembrane helix 5) in the adjacent protomer.

13 DNA and to affect catalysis in the opposing protomer.

14 h asymmetric contributions from each Spatzle protomer.

15 40) N-linked glycan on the other independent protomer.

16 the TREX1 R62A substitution in the opposing protomer.

17 ull catalytic activity in the opposing TREX1 protomer.

18 ts heterotypic interaction with the alpha121 protomer.

19 tinctly regulated compared with the receptor protomer.

20 d Met44, located in subdomain 2 of the lower protomer.

21 stitutions enhanced binding to the truncated protomer.

22 ements in the transport channel of each FocA protomer.

23 y the D1-D2 linker region of its neighboring protomer.

24 d action of residues from more than a single protomer.

25 f expression of the constitutively expressed protomer.

26 regulator SczA, and binds two zinc ions per protomer.

27 rimers with transmembrane pores through each protomer.

28 one protomer is sensed by a second symmetric protomer.

29 of the C-terminal helix alpha9 of the second protomer.

30 e lig1 state and isotopic labeling of either protomer.

31 ntaining F surface residues on a neighboring protomer.

32 ne 5'-O-(3-thiotriphosphate) (ATPgammaS) per protomer.

33 recognize a conserved cavity formed by two F protomers.

34 ximal stimulation required occupancy of both protomers.

35 n a protomer and mediates key contacts among protomers.

36 omeric state composed of two subunits of six protomers.

37 tion through contacts made with two adjacent protomers.

38 moieties interact with different KstR2(Mtb) protomers.

39 o the HA stem to covalently bridge the three protomers.

40 the HSS contributes to communication between protomers.

41 C-terminal (CTD) domains of its successive N protomers.

42 bind to the alpha subunit of pump alphabeta protomers.

43 between the zinc-binding domain and adjacent protomers.

44 eterminants of the interactions between NccX protomers.

45 ch acts as a physical brace between adjacent protomers.

46 otomers and the new finding of cephalosporin protomers.

47 at the interface of adjoining triple helical protomers.

48 ve and negative cooperativity among its four protomers.

49 -arrestin interaction compared with receptor protomers.

50 ins and restricts internal dynamics of RAD51 protomers.

51 hange of N-terminal beta-strands between two protomers.

52 NA affinity, or possibly association of MepR protomers.

53 ments and domains must operate on individual protomers.

54 d signaling behaviors compared with receptor protomers.

55 nts and membrane domains as intact groups of protomers.

56 back onto the E2 by contacts from both RING protomers.

57 transitions of single, fluorescently labeled protomers.

58 oxylate is shifted to the inner TMH of the c-protomers.

59 studies identify allosteric pathways between protomers.

60 eractions within and between the constituent protomers.

61 HA trimer stem at the interface between two protomers.

62 n its surface and the C terminus of adjacent protomers.

63 sharing critical residues from two defective protomers across the heteromer interface.

64 ver, we rationalize how the cross-talk among protomers across the trimerization interface might lead

65 The hIKKbeta protomer adopts a trimodular structure that closely rese

66 eptor (nAChR), whereas its reduction in both protomers almost prevents alpha7 nAChR recognition.

67 IV chains are organized into three canonical protomers alpha121, alpha345, and alpha565 forming three

68 ilic cavity opening to the cytoplasm in each protomer and ending in the middle of the membrane at the

69 interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second prot

70 the first chemical evidence for an alpha565 protomer and its heterotypic interaction with the alpha1

71 with the first triple-helix bundle within a protomer and mediates key contacts among protomers.

72 r and glycans from both subunits of a second protomer and represents a neutralizing epitope that is d

73 mutated PTHR bind retromer through the VPS26 protomer and sequentially assemble a ternary complex wit

74 the N-terminal conformational change of one protomer and the displacement of the C-terminal helix al

75 s was unaffected by induction of the partner protomer and the level of expression of the partner requ

76 pying equivalent hydrophobic pockets in each protomer and their CoA moieties adopting non-equivalent

77 zation differs between the strand-separating protomer and those bound to the single-stranded region.

78 We biochemically reconstituted NPC core protomers and elucidated the underlying protein-protein

79 at the filament contains between 7 and 9 Arp protomers and is capped at both ends.

80 0 homologs, is due to buckling of one of the protomers and is most pronounced at the broadly conserve

81 t the maturation complex is composed of four protomers and one IHF heterodimer bound at the cos site.

82 into final protein products, and assembly of protomers and pentamers in infected M1-D macrophages did

83 The needle is assembled from PrgI needle protomers and the needle tip is capped with several copi

84 otomers, including the known fluoroquinolone protomers and the new finding of cephalosporin protomers

85 tA motif, connecting the active sites of two protomers and thereby modulating the cooperative interac

86 nvestigate the organization of GspC and GspD protomers and to map their interaction sites within the

87 r is nearly identical to that of the F-actin protomer, and in vitro polymerization assays show that t

88 374, located within subdomain 1 of the upper protomer, and Met44, located in subdomain 2 of the lower

89 to the heavy and light chains of mature MPO protomers, and (iii) three covalent bonds between heme a

90 helix folds and AAA+ modules of neighbouring protomers, and a quasi-spiral arrangement of DNA binding

91 als that the antibody binds between two gp41 protomers, and neutralizes the virus by accelerating tri

92 contact peptide residues from all three Env protomers, and thus explains its highly trimer-specific

93 e CARD and the WD40 repeats of a nearby Dark protomer are indispensable for Dronc activation.

94 Additionally, we found that kinase protomers are allosterically coupled, conveying inhibiti

95 otein (TatT) is a water-soluble trimer whose protomers are each perforated by a pore.

96 The gp120 protomers are rotated and separated in the CD4-bound str

97 est that interactions between these family A protomers are too weak to directly influence subcellular

98 that tagged beta(2) adrenergic and mu-opioid protomers are unable to corecruit untagged protomers int

99 To validate our structure, we probed the protomer arrangement by solvent paramagnetic resonance e

100 le conformer simulations of crystallographic protomers as described in the companion article.

101 in human cells have established that septin protomers assemble into linear hetero-octameric rods wit

102 eport the structure of HpUreI, revealing six protomers assembled in a hexameric ring surrounding a ce

103 This protomer assembles into a functional higher-order comple

104 model that describes the effects of salt on protomer assembly into a tetrameric complex.

105 amics in ligand binding, enzyme activity and protomer assembly.

106 le possible helix interfaces mediating inter-protomer associations.

107 ate was crosslinked in vivo to a second SecA protomer at its 1M6N interface, suggesting that this spe

108 trate/inhibitor-binding site of the opposite protomer at its carboxyl terminus.

109 y arms radiating from the sides of the gp120 protomers at a range of angles and place the antibody-bo

110 that assessed interactions between receptor protomers at the surface of transfected cells indicated

111 pposite sides of a nucleosome, but how these protomers avoid competition is unknown.

112 bound to its site has to recruit additional protomers before it can cut DNA.

113 tions, leading us to hypothesize that ScDmc1 protomers bind both cations in the active Dmc1 filament.

114 Two protomers bind the single-stranded region of RNA substra

115 al contact results in one of the independent protomers binding the first GlcNAc of the Asn(340) N-lin

116 The isolated protomer binds DNA weakly and does not discriminate betw

117 XRCC4 phosphorylation and that only one PNKP protomer binds per XRCC4 dimer.

118 in which the binding of a single CTS to one protomer blocks all pumping activity.

119 ve long-range attractive force on individual protomers, both long-range lipid order and interface for

120 ict bends the helices until the helix of one protomer breaks to relieve the repulsion.

121 The N-terminal subunit of each S protomer, called S1, folds into four distinct domains de

122 Specifically, results suggest that D3 protomers can interact with each other via at least two

123 n identity nucleotide (U), whereas the other protomer cleaves RNA between nucleotides +1 and +2.

124 Each protomer comprises six transmembrane segments (TMs), wit

125 During catalysis, the protomer conformational exchange rate becomes enhanced,

126 The trimeric ZneA structures capture protomer conformations that differ in the spatial arrang

127 .3 mol of iron and sulfur, respectively, per protomer (consistent with the presence of a 2Fe-2S clust

128 he enzyme (AF2299) is a homodimer, with each protomer consisting of six transmembrane helices and an

129 Displacement of cis-protomer contacts from the apo state is rate-limiting fo

130 crystallized as a symmetric dimer, with each protomer containing a putative proton channel.

131 Tsr is a homodimer with each protomer containing an L30e-like amino-terminal domain (

132 meric toroid formed by five dimers with each protomer containing one [4Fe-4S] cluster and one Mn(2+)

133 MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four t

134 UT-B is a homotrimer and each protomer contains a urea conduction pore with a narrow s

135 echocystis, showing a tetramer in which each protomer contributes two helices to a membrane-spanning

136 We show that IHF and the terminase protomer cooperatively assemble at the cos site and that

137 key residues in substrate translocation and protomer crosstalk.

138 model to all 3,757 ordered residues in each protomer, defining the transmembrane pore in unprecedent

139 pocket induces a 13 degrees rotation of the protomers, destroying the peg-in-hole R-state interface.

140 Inter-protomer distance correlates with rotation of an alpha-h

141 studies, oligomers are assembled using inter-protomer distance restraints.

142 rast, tagged metabotropic glutamate receptor protomers do corecruit untagged protomers into such micr

143 elective reduction of Cys(26)-Cys(30) in one protomer does not affect the activity against the alpha7

144 6-MDa molecular mass assembly containing six protomers each of two different subunits, Fas1 (beta) an

145 The channel comprises two protomers, each containing two distinct pore domains, wh

146 Each protomer encloses a channel formed by a twisted bundle o

147 These were found to consist of adjacent protomers engaging the interdomain linker of one molecul

148 These mAbs recognize an inter-protomer epitope in the GP fusion loop, a critical and c

149 dimers, ligands bind and activate the 5-HT2C protomer exclusively.

150 The tetramer is asymmetric, three of the protomers exhibiting a closed conformation, and one an o

151 al exchange rate becomes enhanced, the empty protomer exhibits increased local disorder, and water eg

152 The two receptor protomers, extracellular domain and amino terminal fragm

153 Each protomer features a N-terminal zinc finger domain and an

154 antiparallel coiled-coil homodimer with each protomer folded into a helix-loop-helix structure.

155 dimer interface and cap domain, priming one protomer for substrate binding.

156 Thirteen protomers form a large periplasmic domain of six stacked

157 We observe that KIT protomers form close contacts throughout the entire stru

158 in longitudinally between two adjacent actin protomers forming what is called a decorative interactio

159 at completes the active site from a distinct protomer, forming contacts with the gamma-phosphate of t

160 a well-established phenomenon that can alter protomer function.

161 e a model for transport mechanism where CmeB protomers function independently within the trimer.Multi

162 in pleiotropic signaling, yet how individual protomers function within oligomers remains poorly under

163 , because of allosteric interactions between protomers, functionality.

164 These dimers ("protomers") further assemble into a low-rise left-handed

165 ion, allowing the DAD to bind adjacent actin protomers, further disrupting filament structure.

166 tion step occurred sequentially in the three protomers, generating two asymmetric oligomer intermedia

167 The polypeptide fold of the RV capsid protomer has not been observed previously.

168 For this purpose, differently labeled protomers have been assembled into the full pentamer com

169 Each protomer in GltPh consists of a trimerization domain inv

170 s with an N160 glycan from an adjacent gp120 protomer in the antibody-trimer complex.

171 TPases, buries the carboxyl terminus of each protomer in the central channel of the hexamer and hinde

172 coelicolor GlgEs, reported before, with each protomer in the homodimer comprising five domains.

173 trometry indicated that a loss of 4-5 kJ/mol/protomer in the N3 domain that is peripheral to the memb

174 2 may be a result of the optimal bridging of protomers in a putative MOR-mGluR5 heteromer.

175 specific spatial organizations of individual protomers in complexes where the ratiometric composition

176 ofilin has been shown to bridge two adjacent protomers in filamentous actin (F-actin) and promote the

177 ue for dissecting interactions of individual protomers in homo-oligomeric complexes.

178 inhibits all RAF isoforms and occupies both protomers in RAF dimers.

179 eta-strand previously shown to cross between protomers in the closed state.

180 rences are observed at the interface between protomers in the crystal structure of the PCNA-K20ac rin

181 in-swapped, cross-armed conformation for the protomers in the dimeric protein.

182 e curves indicated that the occupancy of the protomers in the Env trimer governs viral activation ver

183 nd always corresponds to nH=N (the number of protomers in the oligomer) for concerted transitions as

184 a strict division of labor between the Ded1p protomers in the oligomer.

185 r several antibiotic species due to multiple protomers, including the known fluoroquinolone protomers

186 tions with the C-terminal alpha-helix of one protomer interacting with the cytoplasmic surface of a s

187 ap stabilizes the closed state through trans-protomer interactions.

188 Both the channel and the protomer interface contain residues conserved in the Ami

189 could identify specific interactions at the protomer interfaces, if the sensitivity is enhanced by d

190 local conformations, and the multiplicity of protomer interfaces, makes the AXH domain an unusual exa

191 novel structure, the NEET fold, in which two protomers intertwine to form a two-domain motif, a cap,

192 cruiting subsets of affinity-tagged family A protomers into artificial microdomains on the surface of

193 d protomers are unable to corecruit untagged protomers into microdomains.

194 ate receptor protomers do corecruit untagged protomers into such microdomains, which is consistent wi

195 The lambda-terminase protomer is composed of one large catalytic subunit tigh

196 The protomer is composed of two domains (N-terminal and C-te

197 The binding of six nucleotides per protomer is consistent with the "rule of six" that gover

198 One protomer is in the outside-facing state.

199 distinct, asymmetric conformation, where one protomer is reconfigured via a helix swap at the middle:

200 l allostery, in which a binding event in one protomer is sensed by a second symmetric protomer.

201 expression we find that BRET between beta2AR protomers is directly proportional to the density of the

202 ers and that the interaction of the receptor protomers is dynamic.

203 loops at the trimeric interface of adjacent protomers is evident in the N197Q mutant by hydrogen-deu

204 ropose a transport mechanism where each CmeB protomers is functionally independent from the trimer.

205 The communication between the two protomers is mediated by an alpha-helix that interacts w

206 e that strong coordination between the motor protomers is required for DNA packaging and that incorpo

207 ve or independent, ATP hydrolysis on the two protomers is sequential and deterministic.

208 In this approach, the predetermined protomer model is subject to full angular and spatial se

209 nifying mechanism to keep the capsid protein protomer monomeric prior to encapsidation of viral RNA.

210 , is highly cooperative indicating that both protomers move in concert.

211 rface of living cells and asking if untagged protomers move into these domains (are corecruited) at t

212 ing-access conformational cycles within each protomer, namely one for protons in the transmembrane re

213 substrate binding and demonstrate that each protomer needs access to both conformations.

214 king existing NPCs and newly synthesized NPC protomers (nups) through anaphase, we uncovered a pool o

215 y demonstrated that SB269652 (1) engages one protomer of a dopamine D2 receptor (D2R) dimer in a bito

216 (SB269652) (1) adopts a bitopic pose at one protomer of a dopamine D2 receptor (D2R) dimer to negati

217 phosphorylation-site mutations into just one protomer of a Y1/Y1 BiFC homodimer had no impact on effi

218 dine tail to include a free cysteine on each protomer of model BG505 NFL trimers to allow covalent li

219 unidirectional transactivation of the 5-HT2C protomer of MT2/5-HT2C heteromers.

220 sides of SecB results in release of only one protomer of SecA yielding a complex of stoichiometry Sec

221 Flexible fitting of a protomer of the EFF-1 crystal structure, which is homolo

222 trimer binding a coupling protein CheW and a protomer of the kinase dimer.

223 ssible counterpart D433 (located on the T1R2 protomer of the receptor) is safely large to avoid elect

224 While the E2 contacts a single protomer of the RING, ubiquitin is folded back onto the

225 hway may lie at or near the interface of the protomers of a BR trimer.

226 ngly suggest that MCC22 acts by bridging the protomers of a MOR-CCR5 heteromer having a TM5,6 interfa

227 prises amino-acid residues from two adjacent protomers of HA.

228 hese RNPs, consisting of approximately 2,600 protomers of nucleocapsid (N) protein, form the template

229 a dimer of dimers, forms a complex with two protomers of SecA, which is the ATPase that provides ene

230 ex that binds Tat substrates, while multiple protomers of TatA assemble at substrate-bound TatBC rece

231 nside a channel-like passage between the two protomers of the dimer.

232 ith the companion subdomain in each brace of protomers of the DnaB hexamer.

233 e only member of the series that bridges the protomers of the heteromer.

234 nd in a wash-resistant manner to one or both protomers of the homodimer.

235 ,164 aa) forms a homodimer and binds to both protomers of the Hsp90 middle domain.

236 in also located within the interface between protomers of trimeric Lg-ECD, thereby explaining the def

237 Structural analyses of distinct segments ("protomers") of the three "channel" nucleoporins yielded

238 sential elements: a monomeric capsid protein protomer, parallel orientation of subunits in the linear

239 lical filament of 103A pitch, comprising 6.4 protomers per turn, with a rise of 16.1A and a twist of

240 omplexes as asymmetric dimers, in which each protomer plays a specific role.

241 d that incorporation of even a single mutant protomer poisons motor activity.

242 assessment of endocytosis of one coexpressed protomer population.

243 apex via contact with two of the three gp120 protomers, possibly contributing to its reported prefere

244 esembles a "nutcracker" with two L-terminase protomers projecting from the C-termini of an S-terminas

245 d by the dimerization arm of the neighboring protomer, providing a structural basis for dimerization

246 One KEN protomer recognizes an identity nucleotide (U), whereas

247 RK1/2 induced by the thrombin-activated PAR1 protomer redistributes to the nucleus.

248 recombinant Saccharomyces cerevisiae Nup157 protomer, representing two-thirds of Nup157 (residues 70

249 alpha7, restricts the proximity of the trans-protomer required for Nt binding.

250 Whereas agonist binding to one protomer resulted in G protein activation, maximal stimu

251 tructure analysis of MAT2B protein (MATbeta) protomer revealed two resveratrol binding pockets, which

252 sidues of the other protomer to disrupt that protomer's TPR-U-box tight binding interface, swiftly ex

253 tomers, with B at its centre, but that these protomers self-associate to assemblies containing severa

254 one DnaK monomer contacts two adjacent ClpB protomers simultaneously.

255 ting how the RAD51-DNA interaction modulates protomer spacing and filament pitch.

256 ting that despite variations in sequence and protomer structure these proteins may share a common pat

257 PIV5-N protomer subdomains are very similar in structure to the

258 ts up differential hydrolysis rates for each protomer, such that the buckled conformation favors ATP

259 ring eight structurally distinct types of IN protomers supporting two catalytically competent subunit

260 nied by a conformational change in the actin protomer that affects filament structure.

261 , both of which contact regions of the actin protomer that are structurally altered by alphaE-catenin

262 ns (alpha1-alpha6), that form triple-helical protomers that assemble into supramolecular networks.

263 efficient molecular recognition between two protomers that become intertwined in their bound state.

264 that are formed by the association of gp140 protomers that differ in amino acid sequence and glycosy

265 Formation of native PulD-multimers by mixing protomers that differ in N3 domain stability, suggested

266 Cross-sensitization of Env protomers that do not bind the CD4mc to neutralization b

267 mation caused by radial and lateral tilts of protomers that leads to bending of the central, pore-lin

268 comprised of three TNF homology domain (THD) protomers that mimic tmTNF.

269 is achieved by coat protein complexes, coat protomers, that bud vesicles from bilayer membranes.

270 motor is composed of a symmetric tetramer of protomers, the maturation complex is better described as

271 s due to pH-dependent allosteric coupling of protomers through two histidines at the dimer interface.

272 rters form homodimers, with each beta-barrel protomer tightly capped by SusD.

273 demonstrating that release requires only one protomer to be functional in stimulating BiP ATPase acti

274 terface into the active site of the opposing protomer to coordinate substrate DNA and to affect catal

275 forces the C-terminal residues of the other protomer to disrupt that protomer's TPR-U-box tight bind

276 nt of the oligomers permits domain 4 of each protomer to move independently as required for catalysis

277 ed region of RNA substrates and load a third protomer to the duplex, which then separates the strands

278 FMNAT catalytic sites of the two neighboring protomers to approach, in agreement with active site res

279 The model shows one of the protomers to be rotated and tilted outward at the tip en

280 ty, resulting in coassembly of mutant and WT protomers to form an enzyme with reduced activity.

281 This complex may incorporate four A(2)B protomers to give the eight catalytic centres (one per A

282 c analyses of the folding of the dimeric HBc protomer under conditions that prevented capsid formatio

283 Two protomers undergo a ratchet-like conformational change t

284 Tubulin protomers undergo an extensive array of post-translation

285 This dominant effect on the associated protomer was also observed in neurons, supporting the ph

286 A physical interaction between the protomers was confirmed using high resolution cryogenic

287 mbinant TRAIL molecule, in which three TRAIL protomers were expressed as a single polypeptide chain (

288 Virus was inactivated when all three Env protomers were occupied by the CD4mc, and gp120 shedding

289 g leads to conformational changes within the protomer, which might propagate within the ring structur

290 n from the monomer to the assembly-competent protomer, which then oligomerizes rapidly to active pore

291 elated rigid body rocking motion of the four protomers, which drives the T to R transition.

292 its, either individually or as part of A(2)B protomers, which indicates that it requires an assembly

293 eotides precisely are associated with each N protomer, with alternating three-base-in three-base-out

294 We show here that BcgI is organized as A(2)B protomers, with B at its centre, but that these protomer

295 onto the exposed helical extension of a Ctf4 protomer within the trimer.

296 toichiometry and relative disposition of the protomers within protein complexes (i.e., quaternary str

297 cific side chain contributions from adjacent protomers within the complex.

298 at the macromolecular interface between two protomers within the trimer.

299 We show unambiguously that individual protomers within the trimeric transporter function fully

300 Each of the four Int protomers, within a multiprotein 400-kDa recombinogenic