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

Research output: Contribution to journalArticlepeer-review

53 Scopus citations

Abstract

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-15N-labeled receptor revealed large backbone motions in the inactive dark state. In contrast, indole side-chain 15N groups of tryptophans showed well resolved, equally intense NMR signals, suggesting restriction to a single specific conformation.

Original languageEnglish (US)
Pages (from-to)3409-3413
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number10
DOIs
StatePublished - Mar 9 2004
Externally publishedYes

ASJC Scopus subject areas

  • General

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