Three-dimensional structure of BmP03 from venom of scorpion Buthus martensii Karsch

被引：0
|
作者：
He, FH [1 ]
Li, YM [1 ]
Wu, G [1 ]
Cao, CY [1 ]
Wu, HM [1 ]
机构：
[1] Chinese Acad Sci, Shanghai Inst Organ Chem, Shanghai 200032, Peoples R China
来源：
ACTA CHIMICA SINICA | 2000年 / 58卷 / 07期
关键词：
scorpion venom; neurotoxin; BmP03; potassium channels; solution structure;
D O I：
暂无
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
From the venom of scorpion Buthus martensii Karsch, a short peptide (BmP03, 28 amino acid residues) was isolated, characterized and tested as a weak inhibitor of K+ channel. In this paper, the solution structure of BmP03 was determined by 2D H-1 NMR spectroscopy and molecular modeling calculations. The conformation of BmP03 is composed of a short alpha - helix (Cys3 - Gly12) and a two - strand antiparallel beta- sheet (Asn16 - Cys19, Cys24 - Asn27). There are three disulfide bridges (Cys3 - Cys19, Cys6 - Cys24, Cys10 - Cys26) connecting the alpha - helix and beta - sheet. Asp20 to Val23 residues form a type II turn linking the two strands. Structural and electrostatic potential comparison between BmP03 and its analogues were also presented.
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页码：850 / 855
页数：6
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