A symmetry-driven search for electrostatic interaction partners in charybdotoxin and a voltage-gated K+ channel

被引：33

作者：

Naini, AA ^{[1
]}

Miller, C ^{[1
]}

机构：

[1] BRANDEIS UNIV,HOWARD HUGHES MED INST,GRAD DEPT BIOCHEM,WALTHAM,MA 02254

来源：

BIOCHEMISTRY | 1996年 / 35卷 / 20期

关键词：

D O I：

10.1021/bi960067s

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A structural model of charybdotoxin bound to a Shaker K+ channel has emerged from mechanistic and mutagenic analysis of toxin-channel interactions. We test this model by predicting through-space electrostatic interactions between specific pairs of channel-toxin residues. Dissociation constants of channel-toxin variants, determined by radiolabeled toxin binding to Shaker-transfected COS membrane fragments, were used to identify pairs of residues located closely enough to interact electrostatically. The results further refine the structural model of the bound complex and produce a more detailed view of the vestibule of the Shaker channel.

引用

页码：6181 / 6187

页数：7

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