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FEBS Lett. 2004 Apr 30;564(3):281-288. doi: 10.1016/S0014-5793(04)00194-2.

The G protein-coupled receptor rhodopsin in the native membrane.

Author information

1
M.E. Müller Institute for Microscopy, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
2
Department of Ophthalmology, University of Washington, Box 356485, Seattle, WA 98195-6485, USA.
3
International Institute of Molecular and Cell Biology, PL-02109 Warsaw, Poland.
4
Department of Pharmacology, University of Washington, Seattle, WA 98195, USA.
5
Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
#
Contributed equally

Abstract

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 microscopy (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.

PMID:
15111110
PMCID:
PMC1393389
DOI:
10.1016/S0014-5793(04)00194-2
[Indexed for MEDLINE]
Free PMC Article

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