Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor α-subunit

被引：29

作者：

Pashkov, VS ^{[1
]}

Maslennikov, IV ^{[1
]}

Tchikin, LD ^{[1
]}

Efremov, RG ^{[1
]}

Ivanov, VT ^{[1
]}

Arseniev, AS ^{[1
]}

机构：

[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia

来源：

FEBS LETTERS | 1999年 / 457卷 / 01期

基金：

俄罗斯基础研究基金会;

关键词：

nicotinic acetylcholine receptor; membrane domain; NMR; conformational analysis;

D O I：

10.1016/S0014-5793(99)01023-6

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 synthetic peptide corresponding to the transmembrane segment M2 (residues 236-267) of the a-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by two dimensional H-1-NMR spectroscopy in a chloroform-methanol (1:1) mixture containing 0,1M LiClO4. Reconstruction of the spatial structure of M2 from the NMR data resulted in an a-helix formed by residues 241-263. Distribution of the molecular hydrophobicity potential on the helix surface is very similar to that in five-helix bundles of proteins with a known three dimensional structure: two hydrophilic bands located on the opposite helix sides separated by strong hydrophobic zones, (C) 1999 Federation of European Biochemical Societies.

引用

页码：117 / 121

页数：5

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