| Literature DB >> 14990789 |
Judith Klein-Seetharaman1, Naveena V K Yanamala, Fathima Javeed, Philip J Reeves, Elena V Getmanova, Michele C Loewen, Harald Schwalbe, H Gobind Khorana.
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 alpha-(15)N-labeled receptor revealed large backbone motions in the inactive dark state. In contrast, indole side-chain (15)N groups of tryptophans showed well resolved, equally intense NMR signals, suggesting restriction to a single specific conformation.Entities:
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Year: 2004 PMID： 14990789 PMCID： PMC373475 DOI： 10.1073/pnas.0308713101
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205