STRUCTURE AND STRUCTURE-FUNCTION-RELATIONSHIPS OF SEA-ANEMONE PROTEINS THAT INTERACT WITH THE SODIUM-CHANNEL

被引：200

作者：

NORTON, RS

机构：

[1] School of Biochemistry, University of New South Wales, Kensington

来源：

TOXICON | 1991年 / 29卷 / 09期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/0041-0101(91)90205-6

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Sea anemones produce a series of toxic polypeptides and proteins with molecular weights in the range 3000-5000 that act by binding to specific receptor sites on the voltage-gated sodium channel of excitable tissue. This article reviews our current knowledge of the molecular basis for activity of these molecules, with particular emphasis on recent results on their receptor binding properties, the role of individual residues in activity and receptor binding, and their three-dimensional structures as determined by nuclear magnetic resonance spectroscopy. A region of these molecules that constitutes at least part of the receptor binding domain is proposed.

引用

页码：1051 / 1084

页数：34

共 131 条

[1] STRUCTURE OF VARIANT-3 SCORPION NEUROTOXIN FROM CENTRUROIDES-SCULPTURATUS EWING, REFINED AT 1.8 A RESOLUTION [J].