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The structural basis of agonist-induced activation in constitutively active rhodopsin

Jörg Standfuss, Patricia C. Edwards, Aaron D’Antona, Maikel Fransen, Guifu Xie, Daniel D. Oprian and Gebhard F. X. Schertler ()
Additional contact information
Jörg Standfuss: Paul Scherrer Institut
Patricia C. Edwards: MRC Laboratory of Molecular Biology
Aaron D’Antona: Brandeis University
Maikel Fransen: Paul Scherrer Institut
Guifu Xie: Brandeis University
Daniel D. Oprian: Brandeis University
Gebhard F. X. Schertler: Paul Scherrer Institut

Nature, 2011, vol. 471, issue 7340, 656-660

Abstract: Rhodopsin activation Structural studies of active states of the visual pigment rhodopsin, a G protein-coupled receptor, have previously been limited to apoprotein or opsin forms that do not contain the agonist all-trans-retinal. Two groups now report structures that reveal more details of the transformations involved in rhodopsin activation. Choe et al. solve the X-ray crystal structure of the metarhodopsin II intermediate of the photoreceptor rhodopsin, and Standfuss et al. determine the structure of a constitutively active mutant of rhodopsin bound to a peptide derived from the C-terminus of the G protein transducin.

Date: 2011
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DOI: 10.1038/nature09795

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