Structure of the sodium channel pore revealed by serial cysteine mutagenesis

被引：95

作者：

PerezGarcia, MT ^{[1
]}

Chiamvimonvat, N ^{[1
]}

Marban, E ^{[1
]}

Tomaselli, GF ^{[1
]}

机构：

[1] JOHNS HOPKINS UNIV, SCH MED, DEPT MED, SECT MOLEC & CELLULAR CARDIOL, BALTIMORE, MD 21205 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1996年 / 93卷 / 01期

关键词：

D O I：

10.1073/pnas.93.1.300

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：

The pores of voltage-gated cation channels are formed by four intramembrane segments that impart selectivity and conductance, Remarkably little is known about the higher order structure of these critical pore-lining or P segments. Serial cysteine mutagenesis reveals a pattern of side-chain accessibility that contradicts currently favored structural models based on alpha-helices or beta-strands, Like the active sites of many enzymes of known structure, the sodium channel pore consists of irregular loop regions.

引用

页码：300 / 304

页数：5

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