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Crystal Structure of Rhodopsin: A G‐Protein‐Coupled Receptor
Author(s) -
Stenkamp R. E.,
Teller D. C.,
Palczewski K.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20021004)3:10<963::aid-cbic963>3.0.co;2-9
Subject(s) - rhodopsin , g protein coupled receptor , chromophore , transmembrane protein , chemistry , biophysics , crystallography , signal transduction , transmembrane domain , membrane protein , receptor , retinal , biology , membrane , biochemistry , photochemistry
Shedding light on GPCRs : The crystal structure of rhodopsin, determined at 2.8 Å resolution, shows the major molecular structural features characteristic of G‐protein‐coupled receptors (see figure). The seven transmembrane helices are aligned roughly perpendicular to the membrane plane, with the binding surface for G proteins located on the cytoplasmic surface. The retinal chromophore important for photon absorption in this vision system protein is completely buried in the protein. The structure of the ground state molecule provides a base for understanding the structural and functional ramifications associated with signal transduction in the retina.