Rhodopsin Forms a Dimer with Cytoplasmic Helix 8 Contacts in Native Membranes

被引：54

作者：

Knepp, Adam M. ^{[1
]}

Periole, Xavier ^{[2
,3
]}

Marrink, Siewert-Jan ^{[2
,3
]}

Sakmar, Thomas P. ^{[1
]}

Huber, Thomas ^{[1
]}

机构：

[1] Rockefeller Univ, Lab Mol Biol & Biochem, New York, NY 10065 USA

[2] Univ Groningen, Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands

[3] Univ Groningen, Zernike Inst Adv Mat, NL-9747 AG Groningen, Netherlands

来源：

BIOCHEMISTRY | 2012年 / 51卷 / 09期

基金：

美国国家卫生研究院;

关键词：

CRYSTAL-STRUCTURE;

D O I：

10.1021/bi3001598

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 HI and H8 contacts is present in native membranes.

引用

页码：1819 / 1821

页数：3

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