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92:
between β11 and β2 and is thereby part of the PR-1 domain. The C-terminal subdomain is stabilized by three disulfide bridges and it is remarkable that this domain does not interact with either the PR-1 domain or the N-terminal sub-domain. The C-terminal subdomain consists of particles, including
88:. This domain is responsible for the selectivity of the protein and consists of two subdomains: N-terminal subdomain (Cys 167 to Cys 179) and C-terminal subdomain (42 amino-acids residues). The N-terminal subdomain is connected with N-terminal domain through two main-chain
104:, Stecrip (88%), Helothermine (49%), Pseudechetoxin (62%), Pseudesin (61%). The snake venoms which belong to CRISP family seem to be homologous to each other, however there are differences in their protein targets.
67:
Triflin is a cysteine-rich secretory protein, which means it belongs to the CRISP family. This is a group of single chain polypeptides found in various organisms. Triflin weighs 25 kDa and consists of 221
273:"Crystallization and preliminary X-ray diffraction analyses of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels"
130:
itself, has high affinity for
Triflin, and may thus work as a defensive mechanism against accidental self-poisoning, suggesting a possible role for SSP-2 as an antidote to triflin.
93:
some hydrophobic residues that are exposed to the solvent. These hydrophobic residues might mediate the interaction with the target proteins and therefore receptor recognition.
190:
Y, Shikamoto; Suto, K; Yamazaki, Y; Morita, T; Mizuno, H (2005). "Crystal structure of a CRISP family calcium-channel blocker derived from snake venom".
320:
Aoki, N; Sakiyama, A; Deshimaru, M; Terada, S (2007). "Identification of novel serum proteins in a
Japanese viper: homologs of mammalian PSP94".
371:
20:
77:
361:
96:
There are some homologous toxins to
Triflin with different percentages of amino-acid sequence similarity, such as
126:
55:
29:
113:
34:
366:
33:). Triflin reduces high potassium-induced smooth muscle contraction, suggesting a blocking effect on
230:
Y. Yamasaki; Koike, H; Sugiyama, Y; Motoyoshi, K; Wada, T; Hishinuma, S; Mita, M; Morita, T (2002).
53:
Triflin is a toxin derived from snake venom. The toxin is produced in the gland of the Habu snake,
112:
Triflin reduces high potassium induced smooth muscle contraction, suggesting a blocking effect on
232:"Cloning and characterization of novel snake venom proteins that block smooth muscle contraction"
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85:
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domain forms an α-β-α sandwich core. This domain is comparable with group 1 plant
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81:
73:
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101:
341:
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257:
211:
45:
160:
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97:
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N, Suzuki; Yamazaki, Y; Fujimoto, Z; Morita, T; Mizuno, H (2005).
44:
24:
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One of the small serum proteins (SSP-2), a substance produced by
322:
139:Other snake venom proteins in the CRISP family:
225:
223:
221:
185:
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181:
179:
8:
296:
247:
72:residues. The first 163 residues of the
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49:Habu snake (Trimeresurus flavoviridis)
7:
23:(CRISP), which is excreted by the
14:
249:10.1046/j.1432-1033.2002.02940.x
21:cysteine-rich secretory protein
1:
192:Journal of Molecular Biology
145:from the Eastern Cottonmouth
78:pathogenesis-related protein
388:
334:10.1016/j.bbrc.2007.05.091
289:10.1107/S1744309105020439
204:10.1016/j.jmb.2005.05.020
127:Trimeresurus flavoviridis
56:Trimeresurus flavoviridis
30:Trimeresurus flavoviridis
27:gland of the Habu snake (
372:Calcium channel blockers
114:L-type calcium channels
35:L-type calcium channels
157:from the Mamushi snake
50:
48:
151:from the Erabu snake
163:from the King Cobra
362:Ion channel toxins
277:Acta Crystallogr F
51:
283:(Pt 8): 750–752.
242:(11): 2708–2715.
86:disulfide bridges
84:domain, has five
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236:Eur. J. Biochem
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198:(4): 735–743.
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90:hydrogen bonds
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367:Snake toxins
328:(2): 330–4.
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80:(PR-1). The
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16:
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356:Categories
170:References
143:Piscivorin
82:C-terminal
74:N-terminal
70:amino-acid
149:Latisemin
120:Treatment
102:Latisemin
63:Chemistry
342:17543280
307:16511147
258:12047379
212:15953617
134:See also
298:1952345
161:Ophanin
155:Ablomin
98:Ablomin
41:Sources
17:Triflin
340:
305:
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108:Target
25:venom
19:is a
338:PMID
303:PMID
254:PMID
208:PMID
330:doi
326:359
293:PMC
285:doi
244:doi
240:269
200:doi
196:350
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281:61
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220:^
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178:^
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202::
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