ライフサイエンスコーパス: His residue

1 sport affinity/selectivity using a conserved His residue.

2 , to hydrogen bond formation with the distal His residue.

3 , and the phosphoryl acceptor in G6Pase is a His residue.

4 t have LanC-like domains have a Lys, Asn, or His residue.

5 elical bending angles close to the conserved His residue.

6 covalently attached to a solvent accessible His residue.

7 inding is reduced by mutation of a conserved His residue.

8 ogonal magnetic orbitals on the cross-linked His residue.

9 might also perturb the pK(a) of the critical His residue.

10 ite, with three of those ligands fitting for His residues.

11 residues and the second of the two conserved His residues.

12 l Zn ligands include conserved Asp, Glu, and His residues.

13 e Er and Rp PKSs, except for the active site His residues.

14 xtensive network of highly conserved Trp and His residues.

15 center formed by an Asn, two Asp, and three His residues.

16 le on aryl fluorosulfates' ability to target His residues.

17 leave at the C-terminal of Ala, Leu, Arg and His residues.

18 idants or through shifting the pKa values of His residues.

19 n HDX reaction rates of Zn-bound and Zn-free His residues.

20 positions occupied by the conserved Phe/Trp/His residues.

21 to form covalent adducts with Lys, Tyr, and His residues.

22 strongly inhibited by Zn(2+), which binds to His residues.

23 n D2O, suggesting assignment to a histidine (His) residue.

24 s indicated that HNE was bound to histidine (HIS) residues.

25 involvement of a localized cluster of three His residues (27, 30, and 180), which comprise a portion

26 avage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously

27 he reciprocal IGF-I substitution Thr(B5) --> His (residue 4) specifies a unique structure with native

28 Substitution of the His residues abolishes PtdIns3P binding by the FYVE doma

29 t were efficiently secreted identified three His residues along with single Asp residue that may play

30 The distal His residues, alpha His58 and beta His63, are protonated

31 Protonation states of 5 equivalent His residues--alpha His20, alpha His50, alpha His89, bet

32 Selected His residues also contribute significantly to UreR funct

33 Whereas substitutions for the three His residues alter metal-binding properties of the prote

34 due is stacked between the metal-coordinated His residue and a relatively conserved aromatic residue.

35 tent with PfHO's lack of a heme-coordinating His residue and suggest an alternative function within p

36 Cu(I) bound in a linear fashion between two His residues and Cu(II) in a square-based pyramid bound

37 Cu(2+) ligand as an imidazole nitrogen of a His residue, and electron-nuclear double resonance (ENDO

38 binds His31, but not any of the other three His residues, and changes the solvent accessibility of r

39 r molecules within 5 A of the catalytic site His residue are included.

40 All five His residues are cationic at pH 4.5, whereas H80 and H95

41 The observed protonation states of His residues are compared to changes in their pK(a) valu

42 residue at position 26, a location at which His residues are found in several cytochrome c homologue

43 Also, two His residues are incorporated with i, i + 5 spacing, des

44 hains, triggers pore formation in vitro, but His residues are nonetheless important for PA functionin

45 Cu reactivity not available in systems where His residues are not adjacent in sequence or space.

46 At pH 7, in contrast, His residues are predominantly neutral, and the Q/H segm

47 At pH 4, where His residues are protonated, the PLD is disordered and f

48 s to Gln sequence variants reveals that both His residues are required for the formation of a well-de

49 For C49A, the remaining Cys and His residues are trans, which facilitates the formation

50 Although His residues are used in coordinating Zn2+ in other prot

51 This supports the proposed role of this His residue as a general base in catalysis.

52 monas enzyme, the low-potential heme has two His residues as axial heme ligands.

53 This model indicated three possible His residues as ligands to inhibitory Cu(2+).

54 The CuM site includes Met(314) and two His residues as ligands.

55 The His residue associates with BChl-a as in the native LH1

56 The variant contains a single misligating His residue at position 26, a location at which His resi

57 nonbinding ATB 2 gamma subdomain contained a His residue at the position occupied by a residue with a

58 Deletion of a His residue at the SU N terminus eliminated the transduc

59 tion factor has been modified to include two His residues at designed i and i+4 positions of its N-te

60 studies indicated the importance of a single His residue because only one was exposed upon removal of

61 )N-substituted protein had Cu(II) bound by 4 His residues, but this coordination changed as the Cu(II

62 Replacement of the amino-terminal His residue by Ala abolishes the ability of KIR2DL1 to b

63 her a Gln, Asn, Glu, Asp, Val, Ala, and/or a His residue by site-directed mutagenesis, using a homolo

64 al base catalyst was identified as a neutral His residue by the DeltaH(ionization) = 7.0 +/- 0.7 kcal

65 of this substitution was to identify crucial His residues by an increase in pH stability of the ligan

66 ct photochemical oxidation of the histidine (His) residue by (1)O2 is a major degradation pathway for

67 osulfate juxtaposing the electrophile with a His residue can be used to afford rapid optimizations of

68 ucine sequences with Asn, Asp, Gln, Glu, and His, residues capable of being simultaneously hydrogen b

69 and Cys114-Cys131), along with three of the His residues critical to catalytic activity (His107, His

70 The in vitro HK activity, the specific His residue-dependent autophosphorylation of the kinase

71 hypothesis that extracellular amino-terminal His residues directly participate in the copper transpor

72 At pH 7, the His residues do not bind RNA or Ca(2+), but do bind Zn(2

73 Our results show that the presence of His residues does not prevent the pH-dependent peptide m

74 rization domain containing the active center His residues (domain A) and the ATP-binding catalysis as

75 roups are analogous to the catalytic Lys and His residues employed during the metal-independent cleav

76 ion (38 amino acids deleted, 23 of which are His residues) expressed partial hydrogenase activity.

77 that pH sensing by evolutionarily conserved His residues facilitates the assembly and packaging of V

78 fully interpreted by backscattering from two His residues (Fe-N at 1.99 A), a bidentate O,O-co-ordina

79 oup, result in autophosphorylation of a DosS His residue, followed by phosphotransfer to an Asp resid

80 e (DEPC) at a mole ratio of 0.74 (DEPC/total His residues) for 3 min at 25 degreesC completely inhibi

81 curs at the dimer interface between pairs of His residues from both monomers.

82 Each heme is coordinated by two His residues from diagonally apposed helices.

83 ely form covalent adducts with Lys, Tyr, and His residues, given that these agents were cell permeabl

84 nesis of the two most likely phosphotransfer His residues (H121 and H168) did not abolish either PDK

85 perone CcmE that binds heme covalently via a His residue (H130 in Escherichia coli) before transferri

86 and abolished by mutating a highly conserved His residue (H292L) predicted to coordinate the cytoplas

87 ides and proteins, we find that all Zn-bound His residues have substantially lower HDX reaction rates

88 A critical His residue (His 58) of LuxU is required for phosphorela

89 A conserved His residue, His(114), is hydrogen-bonded to the Zn(II)-

90 was abolished in mutants lacking both native His residues, His(22) and His(51), but not when either H

91 main, along with the remaining two essential His residues (His242, His244) and Met314, thought to be

92 nducts protons through a critical histidine (His) residue, His37.

93 -like inclusions, and mutation of either one His residue (His570) or one Cys residue (Cys572) within

94 All of these proteins possess Cys and His residues homologous to C161 and H60 of LRAT.

95 amolecular reaction catalyzed by an adjacent His residue in a serine protease-like mechanism.

96 ed interactions, possibly involving the sole His residue in CR2 SCR 1-2.

97 During catalysis, a His residue in G6Pase becomes phosphorylated generating

98 2) Substitution of either His residue in HEXXH leads to apparent intracellular deg

99 binding sites, substitution of the conserved His residue in HpeH abolished kinase activity.

100 ive form that covalently modifies particular His residue in the active site, a difficult task to achi

101 xxxQ motif adjacent to the phospho-accepting His residue in the HisKA_3 subfamily of two-component se

102 vide evidence that mutation of the conserved His residue in the hypothesized catalytic domain results

103 single Glu residue in the S3-S4 linker and a His residue in the pore region each reduced sensitivity

104 trate-assisted catalysis manner, requiring a His residue in the precursor to activate asparagine for

105 The data suggest that the presence of the His residue in the putative transmembrane metal binding

106 or any disease drug target protein bearing a His residue in the vicinity of the active site.

107 uman A(3) receptor at the site of a critical His residue in TM7, previously proposed to be involved i

108 ter with a previously unrecognized conserved His residue in what resembles a metal-ion-binding site.

109 nel is characterized by two or three charged His residues in a tetrad.

110 d this compound is known to modify the three His residues in Abeta proteins by Michael addition.

111 that 4-hydroxy-2-nonenal modifies the three His residues in amyloid beta proteins, which increases t

112 oxidation was used to identify metal-binding His residues in bovine growth hormone (bGH), which has n

113 ry and participation of all three N-terminal His residues in Cu(2+) binding.

114 o permease mutants containing six contiguous His residues in each cytoplasmic loop, inserted factor X

115 bined use of mutants containing 6 contiguous His residues in each periplasmic loop in the permease an

116 y crystallographic data show that the distal His residues in G65T Mb and G65I are positioned approxim

117 Arg302 (helix IX) and Glu325 (helix X) with His residues in permease mutants containing single Cys r

118 ) of histidine, implicating the three native His residues in proton sensing linked to activation.

119 te iron(II) center bound by one Cys and four His residues in the active form of the protein.

120 e agents that covalently target Lys, Tyr, or His residues in the BIR3 domain of the inhibitor of the

121 VWF sequences identified 13 highly conserved His residues in the D1D2D'D3 domains, and His-to-Ala mut

122 nd to Asp1 amine and carbonyl groups and two His residues in the equatorial plane.

123 ts of a novel Zf motif consisting of Cys and His residues in the form Cx8Cx5Cx3H [where x is a variab

124 hat their role is similar to the role of the His residues in the HXGH sequence in class I aminoacyl-t

125 We also found that 3 His residues in the loop appear to temporarily coordinat

126 hat is formed by three icosahedrally related His residues in the N termini of the C subunit at the qu

127 This report addresses the functional role of His residues in the proton-coupled folate transporter (P

128 l His was in a 17-kDa region containing four His residues in the second major sequence homology domai

129 The pKa values of His residues in the studied oligopeptides were found to

130 further pH drop leads to the protonation of His residues in the TM part of the peptide, which induce

131 We conclude that conserved Asp, Glu, and His residues in the transmembrane domains of NixA are cr

132 80% yield and also by the demonstration that His residues in the tripeptides Ala-His-Ala or Ala-Ala-H

133 l pK(a) results for individual Asp, Glu, and His residues in the unfolded drkN SH3 domain.

134 alent dimer and rank the reactivities of the His residues in this protein.

135 figuration to test the importance of the two His residues in TLM and cerulenin binding.

136 Individually mutating each of the five His residues in WT Cx26 did not reveal a key His residue

137 e C terminus, pointing out the importance of His residues in Zn2+ coordination.

138 ttached heme is low-spin, ligated by Met and His residues, in the native state but becomes high-spin

139 We inserted His residues into position 12 or 14 of GWALP23 (replacin

140 ly three His ligands, even though the fourth His residue is conserved.

141 hows that the substitution of Glu-183 with a His residue is detrimental to the chlorination and dismu

142 ggesting that reversible protonation of this His residue is essential.

143 The single His residue is located near a long eight-residue linker

144 The other His residue is stacked between the metal-coordinated His

145 is of the DHFR superfamily revealed that the His residue is the major amino acid component at this po

146 A series of conserved interdomain His residues is identified to be responsible for the pH-

147 utants reveal that the native disposition of His residues is important for conferring growth inhibiti

148 use of electrophiles to specifically target His residues is warranted.

149 on two of the four helices with the Glu and His residues ligating the iron atoms.

150 We examined the role of a His residue located in the M2-M3 extracellular domain (r

151 The pKa values for the two histidine (His) residues located on helix 4 of HPP were determined

152 Removing either the Cys residue or the two His residues lowers the Cu-peptide affinity, but site sp

153 suggest that the protonation of one or both His residues may play a role in the formation of the unf

154 for activation of C3; and a highly conserved His residue (near the C terminus of the one helix that d

155 A conserved His residue of PlcB (His216) that is required for coordi

156 upport from the finding that modification of His residues of band 3 by DEPC reduced I- quenching at p

157 compared with the location of metal-binding His residues of human growth hormone.

158 the effects of mutating the 10 extracellular His residues of mouse gammaENaC.

159 ersible acyl-imidazole pathway linked to the His residues of the beta beta cleft, at a considerably h

160 ier hydrogen bond (LBHB) between the Asp and His residues of the catalytic triad in a serine protease

161 We have replaced the Glu, Asp, and His residues of the yeast PTP to assess their role in th

162 st that the phosphate of the substrate and a His residue on enolase may bind the inhibitory Mg2+.

163 Our data collectively support that a His residue on the protein scaffold polarizes a water mo

164 These His residues (one or both) are therefore essential for Z

165 Of ten His residues, only H247A and H281A mutations altered fun

166 ing consistent with a lower limit of ca. 2-3 His residues per Mn2 core.

167 ich suggests that protonation of one or more His residues (pK(a) ~6.0) mediates the pH dependence of

168 tion and reactivation is about 6, suggesting His residues play a critical role.

169 tophosphorylation site, demonstrate that the His residue plays an essential role in the phosphatase a

170 An analogous His residue present in some CNG channels is an inhibitor

171 for binding an Fe(4)S(4) cluster and Cys and His residues proximate to the loop for binding Ni(II), w

172 sphotransfer proteins (PHPs), which lack the His residue required for phosphorelay.

173 aracterizing binding and dissociation of the His residue responsible for hexacoordination.

174 Site-directed mutagenesis of these His residues results in the loss of RIDalpha-RILP intera

175 dated it by mutation of coordinating Cys and His residues, revealing that a triad of residues (R48C,

176 Mutational analysis of all CooA His residues showed that His77 is critical for CO-stimul

177 Hma, however, lacks conserved His residues shown to mediate haem uptake by other bacte

178 vel amyloid formed by interdigitated Gln and His residue side chains belonging to the prion-like doma

179 y of placing a single pair of His-Asp or Asp-His residues, spaced (i, i + 3), (i, i + 4), or (i, i +

180 ubstituted by Ser, and the alpha-subunit 195(His) residue substituted by Asn.

181 hat catalysis by RadB is enabled by a unique His residue that acts as both the proton donor and accep

182 d that may be predicted to correspond to the His residue that binds one of the accessory bacteriochlo

183 His residues in WT Cx26 did not reveal a key His residue that conferred sensitivity to pH or Zn(2+).

184 To identify the His residue that covalently bound the phosphate moiety,

185 We further found that a His residue that is unique to the chain reversal region

186 harbors the N and C termini residues and two His residues that are implicated in protein splicing.

187 n method, MetalDetector, to identify Cys and His residues that bind to transition metals for the redu

188 ace identified the importance of two CPXV203 His residues that confer low pH stabilization of the com

189 Three His residues that have been identified as Cu(II) ligands

190 f evidence for EKODE modification of protein His residues, the reactions of Nalpha-benzoyl-L-histidin

191 pH dependency is due to a pair of conserved His residues, the successive protonation of which is req

192 en peroxide (H2O2) leads to oxidation of two His residues thereby leading to derepression.

193 onstrated that substitution of Asp-362 for a His residue, thereby reconstituting the canonical metzin

194 ched by interactions with Trp, Tyr, Met, and His residues through a combination of static and dynamic

195 C-MBD, these appear coordinated primarily by His residues thus, suggesting that the three Zn2+ bindin

196 His residue with the side chain of a second His residue to create a T-shaped arrangement of nitrogen

197 n by individually mutating one metal-binding His residue to Cys to allow independent monitoring of th

198 Substitution of the P(-2) His residue to other amino acids produces slow processin

199 ay involve direct coordination of the distal His residue to the heme iron to produce bishistidinyl co

200 nd affects PAM trafficking by mutating these His residues to Ala (Ala-Gly-Ala-Ala; H3A).

201 nine chlorophylls (Chls) and three potential His residues to extra Chls.

202 However, site-specific mutagenesis of eight His residues to Gln identified His145 and His280, but no

203 ermodynamic stability than CYC-2.1 and lacks His residues to misligate to the heme in the protein's d

204 The vast majority of non-Zn-binding His residues undergo no significant changes in HDX react

205 ent in HcRed, we chemically modified Cys and His residues using iodoacetamide and diethyl pyrocarbona

206 The His residue was also relocated throughout the TonB TMD.

207 pacity of 2 more inteins without penultimate His residues was examined.

208 pyrocarbonate (DEPC) showed that one or more His residues was specifically required.

209 for the functional role of the third-member His residue, we have carried out structural and biochemi

210 ng mutations in each conserved Asp, Glu, and His residue were evaluated.

211 The reactivities of these His residues were correlated with solvent accessibility-

212 The protonation states of 35 of the 38 His residues were directly determined from neutron scatt

213 The coordinated His residues were identified by a unique use of Cu(2+)-i

214 When these His residues were substituted for Lys, the positively ch

215 he oxidation of E. coli protein in which all His residues were uniformly labeled with 14C gave rise t

216 In this approach, six histidine (His) residues were incorporated at the C-terminal of the

217 y react with the side chains of Lys, Tyr, or His residues, when properly juxtaposed by a high-affinit

218 -c HS species by protonation of the proximal His residue, whereas the 5-c HS** species lacks the prox

219 is characterized by eight conserved Cys and His residues which form two Zn2+-binding sites termed Si

220 In this study the two T3 Cu coordinating His residues which lie in this pathway in Fet3 have been

221 mes that guanylylate a conserved active site His residue with GDP-L-galactose, forming L-galactose 1-

222 amino group and side chain of the N-terminal His residue with the side chain of a second His residue

223 nitrite structure, replacement of the distal His residue with Val alters the binding mode of nitrite

224 Modification of His residues with diethyl pyrocarbonate completely inhib

225 the necessity for a second highly conserved His residue within the beta subunit.

226 A His residue within the extracellular domain of gammaENaC

227 Mutation of a His residue within the palm subdomain (gammaH88A) abolis

228 ations of two alpha, two beta, and two gamma His residues within extracellular domains significantly

229 These data reinforce the premise that His residues within the Abeta channel sequence are in th

230 ree conserved Asp residues and two conserved His residues yielded a protein that could not be secrete