REFINED STRUCTURE OF CHARYBDOTOXIN - COMMON MOTIFS IN SCORPION TOXINS AND INSECT DEFENSINS

被引：354

作者：

BONTEMS, F

ROUMESTAND, C

GILQUIN, B

MENEZ, A

TOMA, F

机构：

[1] Département d'Ingénierie et d'Etudes des Protéines, CEN Saclay

来源：

SCIENCE | 1991年 / 254卷 / 5037期

关键词：

D O I：

10.1126/science.1720574

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K+ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel beta-sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.

引用

页码：1521 / 1523

页数：3

共 20 条

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