A unified nomenclature for short-chain peptides isolated from scorpion venoms:: α-KTx molecular subfamilies

被引:360
作者
Tytgat, J
Chandy, KG
Garcia, ML
Gutman, GA
Martin-Eauclaire, MF
van der Walt, JJ
Possani, LD
机构
[1] Univ Leuven, Toxicol Lab, B-3000 Louvain, Belgium
[2] Univ Calif Irvine, Dept Phys & Biophys & Med, Irvine, CA 92697 USA
[3] Merck Res Labs, Dept Biochem & Biophys, Rahway, NJ 07065 USA
[4] Univ Calif Irvine, Dept Microbiol & Mol Genet, Irvine, CA 92697 USA
[5] Univ Mediterranee, CNRS, UMR 6560, Biochem Lab, F-13916 Marseille, France
[6] Potchefstroom Univ Christian Higher Educ, Dept Physiol, ZA-2520 Potchefstroom, South Africa
[7] Inst Biotechnol, Dept Mol Recognit & Struct Biol, Cuernavaca 2001, Morelos, Mexico
关键词
D O I
10.1016/S0165-6147(99)01398-X
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Peptidyl toxins are used extensively to determine the pharmacology of ion channels. Four families of peptides have been purified from scorpion venom. In this article, the classification of K+-channel-blocking peptides belonging to family 2 peptides and comprising 30-40 amino acids linked by three or four disulfide bridges, will be discussed. Evidence is provided for the existence of 12 molecular subfamilies, named alpha-KTx1-12, containing 49 different peptides. Because of the pharmacological divergence of these peptides, the principle of classification was based on a primary sequence alignment, combined with maximum parsimony and Neighbour-Joining analysis.
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收藏
页码:444 / 447
页数:4
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