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Journal/Book: Proceedings of the National Academy of Sciences of the United States of America
Published: 2004
Pages: 3409 - 3413
Volume: 101
Issue: 10
Accession no.: 74

Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR

Judith Klein-Seetharaman, Naveena V K Yanamala, Fathima Javeed, Philip J Reeves, Elena V Getmanova, Michele C Loewen, Harald Schwalbe, H. Gobind Khorana
G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the best-studied member of this superfamily. Here, we provide the first evidence that activation in rhodopsin may involve differential dynamic properties of side-chain versus backbone atoms. High-resolution NMR studies of α-N-labeled receptor revealed large backbone motions in the inactive dark state. In contrast, indole side-chain N groups of tryptophans showed well resolved, equally intense NMR signals, suggesting restriction to a single specific conformation.
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Prof. Dr. Harald Schwalbe
Institut für Organische Chemie und Chemische Biologie
Johann Wolfgang Goethe Universität
Max-von-Laue-Str. 7
D-60438 Frankfurt am Main
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