ライフサイエンスコーパス: three-helix bundle

1 xin 1a was discovered, comprising the entire three-helix bundle.

2 olding kinetics of alpha3D, a small designed three-helix bundle.

3 inal extension and is separate from the core three-helix bundle.

4 inal helix-loop-helix motif and a C-terminal three-helix bundle.

5 extends the protein ends away to shrink the three-helix bundle.

6 BA(2) showed that the domain forms a compact three-helix bundle.

7 presumably, 5+ ions to form a highly stable three-helix bundle.

8 e protein adopts the designed structure of a three-helix bundle.

9 and unfolding of a fast-folding, 46 residue three-helix bundle.

10 ty by interacting with other residues in the three-helix bundle.

11 ions of the polypeptide chain and contains a three-helix bundle.

12 y the topological mirror image of the native three-helix bundle.

13 lever arm of the motor and show that it is a three-helix bundle.

14 lpha-helical domain of CusB is folded into a three-helix bundle.

15 ese residues are exposed on the surface of a three-helix bundle.

16 Each subunit consists of a three-helix bundle.

17 trate binding and catalysis and a regulatory three-helix bundle.

18 lar coiled-coil PhoU domains, each forming a three-helix bundle.

19 an N-terminal beta-sandwich and a C-terminal three-helix bundle.

20 structural fold composed of two repeats of a three-helix bundle.

21 g motif of the GGA1 GAT domain consists of a three-helix bundle.

22 lds as a hook-like structure composed of two three-helix bundles.

23 G(B) has an alpha/beta fold, and A(B) is a three-helix bundle (3-alpha).

24 GTPase domain (GD) and the first and second three helix bundles (3HBs) in the middle domain.

25 h to minimizing the Z-domain of protein A, a three-helix bundle (59 residues total) that binds tightl

26 In this respect, the three-helix bundle acts as a template for formation of h

27 E2, showing that SopE2(69-240) comprises two three-helix bundles (alpha1alpha4alpha5 and alpha2alpha3

28 (rubredoxin), and a computationally designed three-helix bundle (alpha3D).

29 residues belonging to both the NPM1 terminal three-helix bundle and a lysine-rich unstructured tail,

30 lpha3DH3 folds into a stable single-stranded three-helix bundle and binds Zn(II) with high affinity u

31 es can bind the MPER when the TM domain is a three-helix bundle and this presentation could influence

32 n-binding site, including one surface of the three-helix bundle, and nearby portions of the sandwich

33 hat the two-pheromone families have the same three-helix bundle architecture.

34 at hydrophobic residues in the centre of the three-helix bundle are crucial for capsid assembly and s

35 ion requires the juxtamembrane middle domain three-helix bundle, as does efficient GTPase activity.

36 35 amino acids, which make a stable dimeric three-helix bundle at low temperatures.

37 ives good fits for the denaturation of Oas's three-helix bundle B domain of protein A (F13W*) and syn

38 The NPM1-C70 terminal three-helix bundle binds the G-quadruplex DNA at the int

39 ty reveal that although the formation of the three-helix bundle by the DeltaL1 TEAD DBD is sufficient

40 examined, t-SNARE function is provided as a three-helix bundle complex containing three approximatel

41 l structure of LIMP-2 displays a hydrophobic three-helix bundle composed of helices 4, 5, and 7, of w

42 sis of the CC at 2.4 A resolution revealed a three-helix bundle, consistent with the formation of bot

43 , more stable udp-bound form that features a three-helix bundle containing a canonical helix-turn-hel

44 It forms a three-helix bundle containing a helix-turn-helix DNA bin

45 s between the SARA beta strand and the Smad2 three-helix bundle contribute significantly to binding a

46 t2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other struc

47 This non-covalent three-helix bundle domain is homologous in structure and

48 The elongated three-helix bundle domains spectrin R16 and R17 fold som

49 hybrid Ig, carbohydrate binding module, and three-helix bundle domains, arranged in a distinctive V-

50 tivator with a unique fold consisting of two three-helix bundle domains.

51 SpA includes five small three-helix-bundle domains that can each bind with high

52 two-state folder, while a longer helix and a three-helix bundle exhibit downhill and two-state transi

53 Surprisingly, the three-helix bundle exhibits a dynamic N-terminal region,

54 The p47 UBA domain has the characteristic three-helix bundle fold and forms a highly stable comple

55 Although the three-helix bundle fold is conserved among acyl carrier

56 While there is conservation of the three-helix bundle fold, Dcp has a higher enthalpy of un

57 sordered and a C-terminal subdomain having a three-helix bundle fold, potentially providing an actin-

58 e C-terminal subdomain that exhibits a novel three-helix bundle fold.

59 olic domain containing a GTPase module and a three-helix bundle followed by two transmembrane (TM) se

60 d 46-56, which are arranged in an up-down-up three-helix bundle forming the edges of a distorted trig

61 BDs from both BAG1 and BAG4 are three-helix bundles; however, in BAG4, each helix in thi

62 Furthermore, each three-helix bundle in the domain-swapped dimer is a stru

63 Similar to Polalpha, p261C of Pol contains a three-helix bundle in the middle and zinc-binding module

64 an elongated asymmetric saddle shape, with a three-helix bundle in the middle and zinc-binding module

65 d targeting proteins to Hsc66, consists of a three-helix bundle in which two helices comprise an anti

66 ed flexibility in residues that link the two three-helix bundles, including the alpha3-alpha4 linker

67 sufficient extension arising from turning a three-helix bundle into a long alpha-helix.

68 ysine-rich sequence at the N terminus of the three-helix bundle is disordered and, although necessary

69 ng site on helices 2 and 3 of the GAT domain three-helix bundle is predicted to interact with coiled-

70 ulin binding sites open up when the domain's three-helix bundle is unfolded and that subsequent calmo

71 third domain of RAP (RAP-D3), which forms a three-helix bundle, is sufficient to reconstitute the es

72 previously identified an activator-targeted three-helix bundle KIX domain in the human MED15 Mediato

73 Here a Calpha-based three-helix-bundle-like protein model with a realistic t

74 rich repeat modules (LRRM), and a C-terminal three-helix bundle (LRRCT).

75 hydrophobic surface patch on the C-terminal three-helix bundle motif of the GAT domain is directly i

76 on of fusion by the long CT or addition of a three-helix bundle occurs at a step preceding initial me

77 ructure, in which the N-terminal part of the three-helix bundle of one repeat packs into the overlapp

78 gment from repeat 2 interacts with the known three-helix bundle of repeat 1 to form a four-helix bund

79 trand, interacts with the beta sheet and the three-helix bundle of Smad2.

80 al analysis demonstrates that the C-terminal three-helix bundle of this GAT domain is responsible for

81 ntennae of the LHC family form transmembrane three-helix bundles of which two helices are interlocked

82 quences of domain swapping from two designed three-helix bundles: one with an up-down-up topology, an

83 PhiF values for the folding of the three-helix bundle, peripheral subunit binding domain fr

84 The model shows that the recently developed three-helix bundle polypeptoids of Lee et al. fold anti-

85 This three-helix bundle presumably interacts with the peripla

86 Here, we describe such simulations of a three helix bundle protein, the engrailed homeodomain (E

87 on simulations of the B and E domains of the three-helix bundle protein A, totaling 60 ns.

88 thermodynamics of an off-lattice model for a three-helix bundle protein are investigated as a functio

89 We study the folding mechanism of a three-helix bundle protein at atomic resolution, includi

90 so here we study the folding pathway of the three-helix bundle protein Engrailed homeodomain.

91 Helices II and III of the three-helix bundle protein form the native helix-turn-he

92 fferent cancers, we computationally designed three-helix bundle protein inhibitors specific for each

93 d maintenance of a tryptophanyl radical in a three-helix bundle protein maquette.

94 Each Trp mutant of the three-helix bundle protein was used as a pseudo-wild-typ

95 and structure determination of alpha(3)D, a three-helix bundle protein with a well-packed hydrophobi

96 ced unfolding of the coiled-coil spectrin (a three-helix bundle protein) for all 20 structures deposi

97 R solution structure of a complex 73-residue three-helix bundle protein, alpha3D, is reported.

98 ding potentials is presented and tested on a three-helix bundle protein, as well as on hairpin and he

99 describe the folding of a simple model of a three-helix bundle protein, we variationally optimize th

100 rize the folding and unfolding of this small three-helix bundle protein.

101 lding thermodynamics of a simple off-lattice three-helix-bundle protein model under equilibrium condi

102 ng a test protein named alpha(3)B-a designed three-helix-bundle protein that forms collapsed, stable

103 -residue villin headpiece subdomain, a model three-helix-bundle protein with a known folded structure

104 hat calculated from a simulation of the same three-helix-bundle protein with an all-atom representati

105 using a coarse-grained model of a family of three-helix bundle proteins whose conformations, once se

106 lied to compute the folding kinetics of four three-helix bundle proteins, all of which fold on a time

107 atomic-level picture of folding mechanics of three-helix bundle proteins.

108 ransitions for various chain lengths and (2) three-helix-bundle proteins A and alpha3C.

109 ains the GTPase domain and the middle domain three-helix bundle serves as a potent, concentration-dep

110 We present the folding of pairs of three-helix bundle spectrin domains as a paradigm to ind

111 The elongated three-helix-bundle spectrin domains R16 and R17 fold and

112 pha-actinin, spectrin, and dystrophin, share three-helix bundle, spectrin repeats that appear in crys

113 otein CT, which has the propensity to form a three-helix bundle, stabilizes the F protein and increas

114 cate that in addition to dissociation of the three-helix bundle stalk domain of prefusion F, the MPER

115 UQ1-UBA forms a compact three-helix bundle structurally similar to other known U

116 he prodomain of MT1-MMP exhibits a conserved three helix-bundled structure and a "bait" loop region l

117 The Ede1 UBA domain forms a three-helix bundle structure and binds ubiquitin through

118 al shifts that are consistent with the known three-helix bundle structure of folded HP35.

119 y tandem homologous motifs with very similar three- helix-bundle structures and similar dimer interfa

120 GGA proteins bind Ub via a three-helix bundle subdomain in their GAT (GGA and targe

121 oove contacts with DNA from either side of a three-helix bundle that binds the DNA major groove.

122 The helical body domain is composed of a three-helix bundle that forms a hydrophobic core with th

123 The B-domain of protein A is a small three-helix bundle that has been the subject of consider

124 atch on helices alpha1 and alpha2 of the GAT three-helix bundle that includes Asn-223, Leu-227, Glu-2

125 ydrophobic repeats in the first helix of the three-helix bundle that makes up each repeat.

126 The MIT domain forms an asymmetric three-helix bundle that resembles the first three helice

127 tral domain that is composed of two extended three-helix bundles that form elongated arms that fold b

128 the core of FCV VPg contains a well-defined three-helix bundle, the MNV VPg core has just the first

129 omains associate to form a fully structured, three-helix bundle, the spectrin tetramerization domain.

130 ociation of a protein loop (wing 2) with the three-helix bundle, thereby enhancing DNA binding.

131 Furthermore, a peptide with a trimeric, three-helix bundle TM domain recapitulates the binding p

132 porated into the backbone of the 36 residue, three-helix bundle villin headpiece subdomain (HP36).

133 previous studies, a domain-swapped, dimeric three-helix bundle was designed from first principles.

134 of CREB binding protein (CBP) forms a small three-helix bundle which folds autonomously.

135 rly structured N-terminal tail followed by a three-helix bundle, which is surprisingly similar to dom

136 e design an antiparallel monomeric untwisted three-helix bundle with 80-residue helices, an antiparal

137 irst structure of TEAD and show that it is a three-helix bundle with a homeodomain fold.

138 d the synaptic t-SNARE complex as a parallel three-helix bundle with a small frayed C terminus.

139 nal domains of CstF-64 and Rna15 fold into a three-helix bundle with an uncommon topological arrangem

140 sembly shows, at the three-fold interface, a three-helix bundle with critical hydrophobic interaction

141 P-binding domain in ARC105 by NMR revealed a three-helix bundle with marked similarity to the CBP/p30

142 sis, the N-terminal region of INCENP forms a three-helix bundle with Survivin and Borealin, directing

143 The RAP domain forms a three-helix bundle with two docking sites, one for each

144 re of the GAT domain of human GGA1 reveals a three-helix bundle, with a long N-terminal helical exten

145 is domain of CagA forms a highly specialized three-helix bundle, with large insertions in the loops c

146 folding simulation, we repeatedly folded the three-helix bundle, with the lowest energy conformations

147 anging from small alpha-helices to a de novo three-helix bundle without biasing the force field towar

148 that mimic several peptides derived from the three-helix bundle "Z-domain" scaffold.