[HTML][HTML] The G protein-coupled receptor rhodopsin in the native membrane
D Fotiadis, Y Liang, S Filipek, DA Saperstein, A Engel… - FEBS letters, 2004 - Elsevier
D Fotiadis, Y Liang, S Filipek, DA Saperstein, A Engel, K Palczewski
FEBS letters, 2004•ElsevierThe 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 …
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 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.
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