ライフサイエンスコーパス: Asp residue

1 hich the beta57Ser residue was changed to an Asp residue.

2 residue Phe137 was replaced by a Glu and an Asp residue.

3 r positions downstream of a highly conserved Asp residue.

4 induced by replacing the native Phe with an Asp residue.

5 ctions would compensate for the loss of this Asp residue.

6 the extent of solvent exposure of the labile Asp residue.

7 in the hydrophobic core with either a Glu or Asp residue.

8 on 190 is used to position the second loop 4 Asp residue.

9 n native and mutant RCs, lacking one or both Asp residues.

10 and consists of conserved Arg, Asn, Lys and Asp residues.

11 lacing the C-terminal Lys residue with three Asp residues.

12 d abolished by replacement with Ala, Arg, or Asp residues.

13 active site region potentially involves two Asp residues.

14 ASE (PIMT) can initiate isoAsp conversion to Asp residues.

15 by a facial triad of two His and one Glu or Asp residues.

16 The protein is rich in His, Glu, and Asp residues.

17 tion site formed, at least in part, by three Asp residues.

18 ts with the carboxylic moiety of these three Asp residues.

19 r fully deprotonating the three coordinating Asp residues.

20 elix alpha3 (residues 594-603) interact with Asp residues 272, 274, 277 and sulfated Tyr residues 278

21 not PI3K was generated by a substitution of Asp residue 395 with Ala.

22 has an unusual substrate site preference for Asp residues, a property that it shares with members of

23 -221) in the NTK with the negatively charged Asp residue abrogated the association between RSK1 and P

24 combinations in positioning of two or three Asp residues along the seven-residue motif of the 2700 p

25 sp-85 in all states and between any [4-(13)C]Asp residue and [14-(13)C]retinal in bR(555) indicates t

26 e all caspases cleave their substrates after Asp residues and are themselves processed from the singl

27 binding domain that is rich in Arg, Glu, and Asp residues and deficient in hydrophobic residues.

28 to change all of the conserved Ser, His, and Asp residues and have found that Ser120, His157, and Asp

29 de conformation, Ca(2+) binds to the charged Asp residues and induces the change of interfiber intera

30 optosis by cleaving key cellular proteins at Asp residues and modifying their function.

31 odels of the MAbs, which included the labile Asp residues and their neighboring amino acid residues.

32 an active site composed of highly conserved Asp residues and two bound hydrated magnesium ions.

33 Mutation of three conserved Asp residues and two conserved His residues yielded a pr

34 followed by proton migration to active site Asp residues, and finally to the leaving pyrophosphate g

35 mediated motility, (ii) two highly conserved Asp residues are crucial for enzymatic activity of the p

36 We conclude that the conserved Asp residues are not equivalent and not all are essentia

37 , and Asp 176; the carboxylate groups of the Asp residues are positioned also to function as the acid

38 Asp residues are present at positions 187 and 226 and ei

39 Several Asp residues are racemized in Abeta plaque, with residue

40 s cleaved by caspase-3 and -7 at a conserved Asp residue (Asp(1109)) in vitro and in epithelial cells

41 active site architecture with a zinc-binding Asp residue (Asp-362).

42 ich was found to be dependent on a conserved Asp residue (Asp-696) within the kinase receiver domain.

43 state behavior to the formation of a charged Asp residue at high pH, and a consequent movement of the

44 Aza-peptide epoxides with an aza-Asp residue at P1 are excellent irreversible inhibitors

45 We propose that the Asp residue at position 246 helps to maintain the proper

46 ice cleaves dSREBP, and cleavage requires an Asp residue at position 386, in the cytoplasmic juxtamem

47 ers slightly from the consensus in having an Asp residue at position 4 (instead of a Glu) and a Thr r

48 nd pK(a) modulation, we introduced a pair of Asp residues at neighboring interior positions of a coil

49 Introduction of Lys or Asp residues at other positions in the putative transmem

50 map two putative caspase-7 cleavage sites to Asp residues at positions 266 and 344 of the ataxin-7 pr

51 h those in 12 known alpha/beta folds and two Asp residues at the C-terminal ends of two adjacent beta

52 Xxx, initiated by the acidic hydrogen of the Asp residue, become significant when ionizing protons ar

53 entate carboxylate oxygens of both conserved Asp residues bridge the two metal ions.

54 Thus, a single Asp residue can account for the sensitivity of Slo2.1 ch

55 etween open and closed conformations plus an Asp residue carboxylate shift between monodentate and bi

56 However, peptides with one or two charged Asp residues close to the center of the hydrophobic sequ

57 Furthermore, two Asp residues, conserved in the majority of Argonaute seq

58 However, although the same Asp residue defines the orientation of the hairpin in bo

59 The specific Asp residue-dependent in vitro phosphotransfer from the

60 Three His and one Asp residues (H79, H238, D246, and H265) are essential f

61 nous release, whereas neutralizing the fifth Asp residue had no effect on the ability of synaptotagmi

62 The Asp residue in each sequence was substituted with Arg, a

63 Desmin is cleaved selectively at a conserved Asp residue in its L1-L2 linker domain (VEMD downward ar

64 Mutation of this Asp residue in nSMase2 disrupts catalysis, allosteric ac

65 Mutating the conserved Asp residue in one of the nine repeats significantly red

66 The pLeu peptide with a Asp residue in the core underwent a pH-dependent transit

67 s with or without a single Ser, Asn, Lys, or Asp residue in the hydrophobic core maintained a transme

68 ies with mutant peptides show that the first Asp residue in the linker sequence helps to stabilize th

69 o the side chain of a functionally important Asp residue in the non-alpha subunit.

70 hat both the charge and the large size of an Asp residue in this position contribute to the severe ef

71 Mutational analysis for all Asp residues in a truncated, fully active MPG protein sh

72 In this work, beta-hydroxylation of Asp residues in EGF domains is demonstrated for a solubl

73 This may relate to the unique involvement of Asp residues in energetically favorable ion pair formati

74 Replacement of these adjacent Asp residues in GerO with Asn reduced the protein's abil

75 nt with the involvement of conserved His and Asp residues in metal binding, and are discussed in the

76 The current study explored the roles of Asp residues in PCFT function.

77 However, in the dehydrated state, Asn and Asp residues in proteins can convert to succinimide resi

78 st likely for the first reaction, 3) the two Asp residues in Section B are essential for the activity

79 mulative electrostatic binding roles for the Asp residues in SSB-Ct.

80 investigate the function of these conserved Asp residues in the ADP-Glc PPase from potato tuber, we

81 Rat caspase-2 also has several Asp residues in the amino and carboxyl cleavage regions

82 ing point substitutions of each of the three Asp residues in the beta' subunit of Escherichia coli RN

83 Leu and Asp residues in the consensus sequence were identified t

84 mational transitions of the peptide with the Asp residues in the doubly protonated, singly protonated

85 ) in which one or two of the three conserved Asp residues in the exonuclease domain are mutated, and

86 ke substitutions for these conserved Gln and Asp residues in the nitrate-responsive NarX sensor and a

87 lved in catalysis, all the conserved Glu and Asp residues in the PDT domain were mutated to Ala.

88 binding site as well as for six of the eight Asp residues in the protease/KNI-272 complex.

89 heet, and usually contains two metal-binding Asp residues in the vWF-A superfamily.

90 ires binding of Ca2+ to the second and third Asp residues in this domain.

91 oncationic peptides containing Ser, His, and Asp residues, including the formation of multilayers.

92 not necessary because mutation of the second Asp residue inhibits Ca2+ binding, yet still allows this

93 sp residues replacing Ser23 and Ser24 or one Asp residue instead of Ser24, indicating that a negative

94 artate aminotransferase, enzymes in which an Asp residue interacts with the pyridine nitrogen of pyri

95 eta-strands carrying two principal catalytic Asp residues into sequential proximity such that unique

96 Results also indicate that the Asp residue is important for both autokinase and transmi

97 A conserved catalytic Asp residue is required for Gdh1's functions in telomeri

98 C215S) while in the second, the general acid Asp residue is substituted by an Ala (e.g., PTP1B/D181A)

99 Differentiation of isoAsp and Asp residues is a challenging task owing to their simila

100 Although one of these Asp residues is absent from the A1, A2, and A3 domains,

101 -chain active enzyme by cleavage at internal Asp residues, it follows that an upstream caspase can pr

102 for suppression, as mutation of a conserved Asp residue, likely to coordinate a metal ion, inactivat

103 Class A GPCRs contain a highly conserved Asp residue located in transmembrane domain II (TM II; c

104 ne-inserted polyLeu-rich peptides containing Asp residues located at various positions in their hydro

105 Mutation of single Asp residues located in the S2 (D456, D460) or S3 (D509)

106 folding/trafficking and may charge-pair with Asp residues located in the S2 and S3 domains.

107 The replacement of two key Asp residues located in the transmembrane part of pHLIP

108 that interactions mediated by the catalytic Asp residues make a major contribution to the tight bind

109 In ZO1-PDZ1, an Asp residue makes favorable interactions with both Tyr(-

110 The geometry of metal binding to these Asp residues may be crucial in determining the catalytic

111 rved Asn residue in the V1 loop of Env to an Asp residue (N-136-->D).

112 bined mutations of two or three of these key Asp residues nearly eliminated the shift induced by 0.5

113 roton association/dissociation at a critical Asp residue of MotB (Asp 32 in the protein of Escherichi

114 The structure also set the identity of the Asp residue of the catalytic triad of Ser, His, and Asp

115 s residue, followed by phosphotransfer to an Asp residue of the response regulator DosR.

116 Moreover, mutation of the three Asp residues of P69, which correspond to the three catal

117 which correspond to the three catalytic site Asp residues of pol beta, inactivated the enzyme without

118 equences, align spatially with the catalytic Asp residues of RNase H-like catalytic sites, suggesting

119 ected mutagenesis of predicted catalytic Ser/Asp residues of RT0522 also eliminates cytotoxicity and

120 5N5) of Dslo-C280, in which five consecutive Asp residues of the "Ca-bowl" motif are changed to Asn,

121 gmin I with mutations in the first or fourth Asp residues of the C2B domain partially rescued synchro

122 Mutating either the second or third Asp residues of the C2B domain potently inhibited the ab

123 e the carboxyl groups of the first and third Asp residues of the DDDD motif, the backbone carbonyl of

124 H-type divalent cation-coordinated catalytic Asp residues of the PIWI domain.

125 wo reentrant loops with the critical His and Asp residues on opposite sides of the endoplasmic reticu

126 the Zn(2+) ion is coordinated by a conserved Asp residue only observed to date as a metal ligand in M

127 Of the 6 other conserved Asp residues, only one, D109, is shown to be required fo

128 , but many members lack either the canonical Asp residue or the DNA binding domain.

129 tered by introduction of negatively charged (Asp) residues, or when the cytosolic domain in the chime

130 An Asp residue projecting into this cleft is essential for

131 ter that is coordinated by three Cys and one Asp residue rather than the expected four Cys.

132 cluster is coordinated by three Cys and one Asp residue, rather than by the typical four Cys residue

133 Of the 5 Glu and Asp residues replaced by Gln or Asn in our experiments,

134 to react with mutants containing either two Asp residues replacing Ser23 and Ser24 or one Asp residu

135 tion site was substituted with either Ala or Asp residues, respectively, correlated with negative pho

136 g domain of GPIIb, with a negatively charged Asp residue resulted in marked reduction in the ability

137 replacement of both Ser-128 and Thr-201 with Asp residues (S128D/T201D) increases Plx1 activity appro

138 The structures highlight an Asp residue separated by two residues from a dileucine s

139 n healthy tissue; at acidic pH, titration of Asp residues shifts the equilibrium toward membrane inse

140 utants with a single mutation at a conserved Asp residue that coordinates Ca(2+)-binding in LDLR repe

141 ntified three His residues along with single Asp residue that may play a role in catalysis.

142 Two conserved Asp residues that coordinate the metal ions, which are a

143 ns of the five negatively charged aspartate (Asp) residues that constitute the Ca2+-binding sites in

144 of H-bonds with only one side chain, from an Asp residue, the amino group of the N-terminal Gly of th

145 nd GerO, but not GerQ contained two adjacent Asp residues thought to be important in the function of

146 d that mutation of these residues to Glu and Asp residues (TNF-R1.4D/E) mimics the effect of phosphor

147 ed, in (HUMAN)NAT2 variants, mutation of the Asp residue to Asn, Gln, or Glu dramatically impairs enz

148 signals by selectively cleaving proteins at Asp residues to alter their function.

149 We mutated each of these conserved Asp residues to Gly individually and in pairs in Gbeta a

150 ases that cleave intracellular substrates at Asp residues to modify their function and promote apopto

151 red in a manner that would allow the charged Asp residues to reside near the bilayer surface.

152 and Ser(86)) were individually replaced with Asp residues to simulate phosphorylation.

153 The role of this Asp residue was investigated using a series of mutants,

154 A single Asp residue was replaced for an Asn side chain at the a-

155 ues while hydrolysis on the carboxyl side of Asp residues was also observed.

156 When Asp residues were ionized (at neutral or high pH), topog

157 When Asp residues were protonated (at low pH), peptides that

158 creased under low pH conditions in which the Asp residues were protonated.

159 of a series of pHLIP variants where the four Asp residues were sequentially mutated to nonacidic resi

160 ence, as well as the conserved Ser, His, and Asp residues which are known to function as the catalyti

161 The mutated Asp residue, which determines the disease phenotype, is

162 ses (PTPases) is accomplished by a conserved Asp residue, which is brought into position for catalysi

163 second TM helix contains a highly conserved Asp residue, which is critical for agonist activation in

164 However, replacement of either Asp residues with Asn eliminates all but a residual leve

165 In contrast, substitution of distal Glu and Asp residues with Gly or their deletion resulted in pro-

166 kcal/mol relative to the protonation of two Asp residues with unperturbed pK(a) values.

167 The invariant His and highly conserved Asp residues within the membrane-bound O-acyltransferase