ライフサイエンスコーパス: His residue

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

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

3 elical bending angles close to the conserved His residue.

4 covalently attached to a solvent accessible His residue.

5 sport affinity/selectivity using a conserved His residue.

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

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

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

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

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

11 xtensive network of highly conserved Trp and His residues.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

28 Selected His residues also contribute significantly to UreR funct

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

114 80% yield and also by the demonstration that His residues in the tripeptides Ala-His-Ala or Ala-Ala-H

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

200 Modification of His residues with diethyl pyrocarbonate completely inhib

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

202 A His residue within the extracellular domain of gammaENaC

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

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

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

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