THE PORE DIMENSIONS OF GRAMICIDIN-A

被引：556

作者：

SMART, OS

GOODFELLOW, JM

WALLACE, BA

机构：

[1] Department of Crystallography, Birkbeck College, University of London

来源：

BIOPHYSICAL JOURNAL | 1993年 / 65卷 / 06期

关键词：

D O I：

10.1016/S0006-3495(93)81293-1

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The ion channel forming peptide gramicidin A adopts a number of distinct conformations in different environments. We have developed a new method to analyze and display the pore dimensions of ion channels. The procedure is applied to two x-ray crystal structures of gramicidin that adopt distinct antiparallel double helical dimer conformations and a nuclear magnetic resonance (NMR) structure for the beta6.3 NH2-terminal to NH2-terminal dimer. The results are discussed with reference to ion conductance properties and dependence of pore dimensions on the environment.

引用

页码：2455 / 2460

页数：6

共 44 条

[1]

ABOLA EE, 1987, CRYSTALLOGRAPHIC DAT, P107

[2]

ANDERSEN OS, 1984, ANNU REV PHYSIOL, V46, P531

[3] ENERGETICS OF ION PERMEATION THROUGH MEMBRANE CHANNELS - SOLVATION OF NA+ BY GRAMICIDIN-A [J].