期刊
FEBS LETTERS
卷 564, 期 3, 页码 281-288出版社
WILEY
DOI: 10.1016/S0014-5793(04)00194-2
关键词
atomic force microscopy; G protein-coupled receptor; membrane protein; photoreceptor cell; rhodopsin; transmission electron microscopy
资金
- NEI NIH HHS [EY01730, R01 EY008061, P30 EY001730, EY08061] Funding Source: Medline
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.
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