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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Fotiadis D,Liang Y,Filipek S,Saperstein DA,Engel A,Palczewski Kdoi
10.1016/S0014-5793(04)00194-2keywords:
subject
Has Abstractpub_date
2004-04-30 00:00:00pages
281-288issue
3eissn
0014-5793issn
1873-3468journal_volume
564pub_type
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