The G protein-coupled receptor rhodopsin in the native membrane

被引:181
|
作者
Fotiadis, D
Liang, Y
Filipek, S
Saperstein, DA
Engel, A
Palczewski, K
机构
[1] Univ Basel, Biozentrum, ME Muller Inst Microscopy, CH-4056 Basel, Switzerland
[2] Univ Washington, Dept Ophthalmol, Seattle, WA 98195 USA
[3] Int Inst Mol & Cell Biol, PL-02109 Warsaw, Poland
[4] Univ Washington, Dept Pharmacol, Seattle, WA 98195 USA
[5] Univ Washington, Dept Chem, Seattle, WA 98195 USA
来源
FEBS LETTERS | 2004年 / 564卷 / 03期
关键词
atomic force microscopy; G protein-coupled receptor; membrane protein; photoreceptor cell; rhodopsin; transmission electron microscopy;
D O I
10.1016/S0014-5793(04)00194-2
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
The higher-order structure of G protein-coupled receptors (GPCRs) in membranes may involve dimerization and formation of even larger oligomeric complexes. Here, we have investigated the organization of the prototypical GPCR rhodopsin in its native membrane by electron and atomic force micros-copy (AFM). Disc membranes from mice were isolated and observed by AFM at room temperature. In all experimental conditions, rhodopsin forms structural dimers organized in paracrystalline arrays. A semi-empirical molecular model for the rhodopsin paracrystal is presented validating our previously reported results. Finally, we compare our model with other currently available models describing the supramolecular structure of GPCRs in the membrane. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:281 / 288
页数:8
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