ELECTROSTATIC DISTANCE GEOMETRY IN A K+ CHANNEL VESTIBULE

被引：83

作者：

STOCKER, M

MILLER, C

机构：

[1] Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 20期

关键词：

CHARYBDOTOXIN; SHAKER; COMPLEMENTARY MUTAGENESIS; PROTEIN ELECTROSTATICS;

D O I：

10.1073/pnas.91.20.9509

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：

Many voltage-gated K+ channels carry in the external vestibule a receptor for charybdotoxin, a peptide channel blocker. We use point mutagenesis of both charybdotoxin and a Shaker K+ channel to isolate the electrostatic interaction energy between chosen pairs of residues, one on the channel and one on bound toxin. The results allow estimates of physical distances between such residue pairs and, in combination with the known structure of charybdotoxin, localize specific channel residues in three-dimensional space.

引用

页码：9509 / 9513

页数：5

共 29 条

[21] DIFFUSION-CONTROLLED BINDING OF A PEPTIDE NEUROTOXIN TO ITS K+ CHANNEL RECEPTOR [J].