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Biochemistry. 2012 Mar 6;51(9):1819-21. doi: 10.1021/bi3001598. Epub 2012 Feb 27.

Rhodopsin forms a dimer with cytoplasmic helix 8 contacts in native membranes.

Author information

1
Laboratory of Molecular Biology and Biochemistry, The Rockefeller University, New York, New York 10065, United States.

Abstract

G protein-coupled receptors form dimers and higher-order oligomers in membranes, but the precise mode of receptor-receptor interaction remains unknown. To probe the intradimeric proximity of helix 8 (H8), we conducted chemical cross-linking of endogenous cysteines in rhodopsin in disk membranes. We identified a Cys316-Cys316 cross-link using partial proteolysis and liquid chromatography with mass spectrometry. These results show that a symmetric dimer interface mediated by H1 and H8 contacts is present in native membranes.

PMID:
22352709
PMCID:
PMC3332060
DOI:
10.1021/bi3001598
[Indexed for MEDLINE]
Free PMC Article

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