期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 10, 页码 3409-3413出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0308713101
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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-N-15-labeled receptor revealed large backbone motions in the inactive dark state. In contrast, indole side-chain N-15 groups of tryptophans showed well resolved, equally intense NMR signals, suggesting restriction to a single specific conformation.
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