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

doi:10.1073/pnas.0308713101

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

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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 language	English (US)
Pages (from-to)	3409-3413
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	101
Issue number	10
DOIs	https://doi.org/10.1073/pnas.0308713101
State	Published - Mar 9 2004
Externally published	Yes

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Klein-Seetharaman, J., Yanamala, N. V. K., Javeed, F., Reeves, P. J., Getmanova, E. V., Loewen, M. C., Schwalbe, H., & Khorana, H. G. (2004). Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR. Proceedings of the National Academy of Sciences of the United States of America, 101(10), 3409-3413. https://doi.org/10.1073/pnas.0308713101

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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.",

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AU - Klein-Seetharaman, Judith

AU - Yanamala, Naveena V.K.

AU - Javeed, Fathima

AU - Reeves, Philip J.

AU - Getmanova, Elena V.

AU - Loewen, Michele C.

AU - Schwalbe, Harald

AU - Khorana, H. Gobind

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N2 - 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.

AB - 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.

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

Abstract

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