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The G protein‐coupled receptor rhodopsin in the native membrane
Author(s) -
Fotiadis Dimitrios,
Liang Yan,
Filipek Slawomir,
Saperstein David A,
Engel Andreas,
Palczewski Krzysztof
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00194-2
Subject(s) - rhodopsin , g protein coupled receptor , paracrystalline , membrane , supramolecular chemistry , membrane protein , biophysics , chemistry , atomic force microscopy , crystallography , receptor , biology , nanotechnology , biochemistry , materials science , crystal structure , retinal
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.