ライフサイエンスコーパス: cystine knot

1 cture by three disulfide bonds, which form a cystine knot.

2 is the presence of a stabilizing C-terminal cystine knot.

3 lpha-helical structures commonly observed in cystine knots.

4 8-82, and 32-84; the last three comprise the cystine knot, a structure also seen in a variety of grow

5 Cystine knot alpha-amylase inhibitors are cysteine-rich,

6 Similar to other knottins, cystine knot alpha-amylase inhibitors are highly resista

7 n together, our results expand membership of cystine knot alpha-amylase inhibitors in the Apocynaceae

8 Here, we show that cystine knot alpha-amylase inhibitors named alstotides d

9 oline bonds, characteristics shared by other cystine knot alpha-amylase inhibitors.

10 toms of several residues in the beta-subunit cystine knot, alpha-subunit loop 2, and the small seatbe

11 harmacologically active C-C-CC-C-C inhibitor cystine knot and CC-C-C motifs (168 and 44 toxins, respe

12 are those contained within the beta-subunit cystine knot and reveal that a disulfide exchange occurr

13 s between backbone atoms of the beta-subunit cystine knot and the tensor loop with backbone atoms in

14 reversibly with parts of the NH(2) terminus, cystine knot, and loop 2 of the hCG beta-subunit.

15 it potentiates formation of the beta-subunit cystine knot, and second, contacts between alpha-subunit

16 o a homogeneous product, retains the desired cystine knot architecture, functions as an antagonist, a

17 Thus, individual bonds of cystine knot are important for secretion and heterodimer

18 e that all three "X" residues within the hCG cystine knots are collectively, but not individually, re

19 Two cystine knots are energetically preferred; however, all

20 ng of panitide L3 showed that it possesses a cystine knot arrangement similar to cyclotides.

21 l end-to-end cyclic backbone combined with a cystine knot arrangement, making them exceptionally stab

22 e leptin receptor contained several distinct cystine knots as well as 10 free cysteines.

23 Whether the two non-cystine knot bonds 7-31 and 59-87 could form independent

24 fide bonds, collectively known as the cyclic cystine knot (CCK) motif.

25 t form a knotted structure known as a cyclic cystine knot (CCK).

26 The C-terminal cystine knot (CK) (CTCK) domain in von Willebrand factor

27 Cystine knots consist of three intertwined disulfide bri

28 receptor associations that are determined by cystine-knot containing subdomains.

29 otein that shares similarity with a class of cystine knot-containing factors including dan, cerberus,

30 CG) is a heterodimeric member of a family of cystine knot-containing proteins that contain the consen

31 insight into the folding mechanisms of other cystine knot-containing proteins.

32 shares 81% identity, macaque (m)CG-beta is a cystine knot-containing subunit that assembles with an a

33 Mutation of non-cystine knot disulfide bond 7-31, bond 59-87, or both (l

34 Furthermore, mutation of the cystine knot disulfide bonds resulted in multiple foldin

35 l receptor ectodomain (ECD) with the Spatzle cystine knot domain dimer.

36 The C-terminal cystine knot domain dimerizes end-to-end in a manner pre

37 by two loops presented by a well-structured cystine knot domain within AGRP(87-132).

38 e AGRP analogue designed to contain only the cystine knot domain.

39 that Hi1a comprises two homologous inhibitor cystine knot domains separated by a short, structurally

40 d here for the first time between the D4 and cystine-knot domains form a stem.

41 factor (VEGF) is a homodimeric member of the cystine knot family of growth factors, with limited sequ

42 uence patterns similar to those found in the cystine knot family of proteins.

43 It is the first member of the cystine knot family to have a defined function in invert

44 is predicted bursicon protein belongs to the cystine knot family, which includes vertebrate transform

45 he cytokine Spatzle, a dimeric ligand of the cystine knot family.

46 ASIP adopts the inhibitor cystine knot fold and, along with AgRP, are the only kno

47 cture with each monomer adopting a conserved cystine knot fold.

48 s similar in structure to IL-17F, adopting a cystine-knot fold.

49 disulfide exchange event crucial for CG-beta cystine knot formation and attainment of CG-beta assembl

50 ariant Gly residue is required for efficient cystine knot formation and subunit folding.

51 ide rearrangement is an essential feature of cystine knot formation during CG-beta folding.

52 Cystine knot formation proceeded through a 1-disulfide i

53 pathway and that 59-87 forms during or after cystine knot formation.

54 Neurotrophin-3 (NT-3) is a cystine knot growth factor that promotes the survival, p

55 mily members adopt a monomer fold typical of cystine knot growth factors, despite lacking the disulfi

56 ain noncovalently associated with the mature cystine-knot growth factor domain after processing.

57 on, to our knowledge the first heterodimeric cystine knot hormone found in insects, consists of two p

58 ucture is consistent with two models for the cystine knot; however, the poor density for the majority

59 the toxin comprises a well-defined inhibitor cystine knot (ICK) backbone region and a flexible C-term

60 8, and are shown to belong to the inhibitory cystine knot (ICK) family of peptide toxins interacting

61 region of AGRP(87-132) adopts the inhibitor cystine knot (ICK) fold previously identified for numero

62 of the three-disulfide-containing inhibitor cystine knot (ICK) motif found widely in animals and pla

63 MR spectroscopy revealed a classic inhibitor cystine knot (ICK) motif.

64 pattern C-C-CC-C-C that forms the inhibitory cystine knot (ICK) or knottin motif.

65 reported to adopt a well-defined inhibitory cystine knot (ICK) scaffold structure.

66 s identified that AGRP contains an inhibitor cystine knot (ICK) structural fold, and that is the firs

67 da venatoria toxin 2 (HpTx2) is an inhibitor cystine knot (ICK)-gating modifier toxin that selectivel

68 These results suggested that the cystine knot is critical for the intracellular integrity

69 The conserved motif of the cystine knot is CX3CP.

70 The cystine knot is N-terminal to the collagen triple helix

71 This novel cystine knot is present in type IX collagen, too.

72 ion to synthesize dimers of integrin-binding cystine knot (knottin) miniproteins with low-picomolar b

73 d illuminated with a fluorescent, engineered cystine knot (knottin) peptide that binds with high affi

74 d to engineer a small, disulfide-constrained cystine knot (knottin) peptide that bound to alpha(v)bet

75 Norrin (Norrie Disease Protein) is a cystine-knot like growth factor.

76 ugh disulfide bonds between their C-terminal cystine knot-like (CK) domains.

77 ons that cystine residues of the hCG subunit cystine knots make in folding, assembly, and bioactivity

78 The cystine-knot miniproteins present in tomato fruit (TCMPs

79 cular disulfide bonds, three of which form a cystine knot motif (10-60, 28-82, and 32-84).

80 ma pruriens, that conforms to the inhibitory cystine knot motif and which modifies activation kinetic

81 residue C-terminal extension with a modified cystine knot motif found in multisubunit external cell s

82 the mutant structures suggests a role of the cystine knot motif in protein folding rather than in the

83 The modified cystine knot motif stabilizes cell-bound trimers upon Ca

84 ein hormone alpha-subunit (GPH-alpha) form a cystine knot motif that stabilizes a three-loop antipara

85 monomeric and consists of an eight-membered cystine knot motif with a fold similar to transforming g

86 tides from three different classes of cyclic cystine knot motif-containing cyclotides: Mobius (M), tr

87 C-term VHv1.1 represents a new and distinct cystine knot motif.

88 de peptide was consistent with an inhibitory cystine knot motif.

89 re, their end-to-end cyclic structure with a cystine-knot motif represents a molecular structure of a

90 ssue growth factor (CCN2/CTGF) to C-terminal cystine knot motifs present in key angiogenic regulators

91 ere substituted by swapping their respective cystine knot motifs, the resulting chimeras appeared to

92 Conversely, the cystine knot mutants were inefficiently secreted (<25%).

93 utants was greater than 95%, whereas for the cystine knot mutants, it was 20-40%.

94 From these studies we conclude that: (i) the cystine knot of GPH-alpha is necessary and sufficient fo

95 The cystine knot of Spz binds the concave face of the Toll l

96 First, the cystine knot of the alpha-subunit potentiates formation

97 d and allows for the proper oxidation of the cystine knot of type III collagen after the short triple

98 was found to adopt the so-called "inhibitor cystine knot" or "knottin" fold stabilized by three disu

99 toxin guangxitoxin-1E (GxTX), an inhibitory cystine knot peptide that binds selectively to Kv2-type

100 These cystine knot peptide tracers, in particular (18)F-fluoro

101 A yeast-displayed cystine-knot peptide library was generated by substituti

102 f the Agouti-related protein (AgRP), a 4-kDa cystine-knot peptide with four disulfide bonds and four

103 ProTx-II and huwentoxin-IV (HWTX-IV), cystine knot peptides from tarantula venoms, preferentia

104 Cystine knot peptides were labeled with N-succinimidyl-4

105 Here, we evaluated 2 cystine knot peptides, R01 and S02, previously engineere

106 Four macrocyclic cystine-knot peptides of 29-31 residues, kalata, circuli

107 Mutant cystine-knot peptides were screened in a high-throughput

108 as characterized recently as a heterodimeric cystine knot protein in Drosophila melanogaster.

109 ligand is the human nerve growth factor-like cystine knot protein Spatzle.

110 e V-ATPase of pea albumin 1b (PA1b), a small cystine knot protein that shows exquisitely selective in

111 ocus on Drosophila bursicon, a heterodimeric cystine-knot protein that activates the G protein-couple

112 We have found that the structurally related cystine-knot protein, nerve growth factor beta (NGFbeta)

113 endoproteinase Lys-C, resulting in a stable cystine-knot protein.

114 ved trio of disulfide bonds shared among all cystine knot proteins, but the remaining two putative di

115 ling and the structure and function of other cystine knot proteins.

116 is a neuropeptide hormone consisting of two cystine-knot proteins (burs alpha and burs beta), respon

117 x ligands, including the family of mammalian cystine-knot proteins.

118 Comparison with other classes of cystine knots provides indication that C-term VHv1.1 rep

119 cule supports the hypothesis that indeed the cystine knot region possesses the melanocortin receptor

120 esidues 991 to 1032 including the C-terminal cystine knot region, to 2.3A resolution.

121 equence of either the alpha- or beta-subunit cystine knot resulted in non-native disulfide bond forma

122 7-31, bond 59-87, or both (leaving only the cystine knot) resulted in an efficiently secreted foldin

123 own as cyclotides that possess a macrolactam-cystine knot scaffold imparting exceptional physiologica

124 cerberus (PRDC) is a secreted protein with a cystine knot structure identified by gene trapping in em

125 GVIIJ[C24S] adopts an inhibitor cystine knot structure, with two antiparallel beta-stran

126 The eight cystine knot topologies that are characterized by exclus

127 ions from several venoms and characterized a cystine knot toxin called JZTx-27 from the venom of tara

128 hypothesize parallel evolution of inhibitor cystine knot toxins from Araneomorphae and Mygalomorphae

129 cysteine-stabilized alpha/beta and inhibitor cystine knot types of fold.

130 hered gonadotropins bearing mutations in the cystine knot was increased significantly.

131 ot disulfide bonds and demonstrated that the cystine knot was necessary and sufficient for efficient

132 d not form when all cysteine residues of the cystine knot were converted to alanine, suggesting that

133 aring single cysteine residue mutants in the cystine knot were significantly reduced.