Structure of rhodopsin and the superfamily of seven-helical receptors: the same and not the same.
The crystal structure of rhodopsin provides significant insights concerning structure/activity relationships in visual pigments and related G-protein-coupled receptors. The specific arrangement of seven-transmembrane helices is stabilized by a series of intermolecular interactions that appear to be conserved among Family A receptors. However, the potential for structural and functional diversity among members of the superfamily of seven-helical receptors presents a significant future challenge.
Sakmar
Thomas P
TP
Howard Hughes Medical Institute, Laboratory of Molecular Biology and Biochemistry, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. sakmar@mail.rockefeller.edu
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D019204:GTP-Binding Proteins / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012176:Retinoids / Q000737:chemistry; D012243:Rhodopsin / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
D012176:Retinoids; C121835:retinylidene chromophore; D012243:Rhodopsin; D019204:GTP-Binding Proteins