Related ArticlesAmino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Biochim Biophys Acta. 2013 Oct 29;
Authors: Pope A, Eilers M, Reeves PJ, Smith SO
Abstract
Rhodopsin is a classical two-state G protein-coupled receptor (GPCR). In the dark, its 11-cis retinal chromophore serves as an inverse agonist to lock the receptor in an inactive state. Retinal-protein and protein-protein interactions have evolved to reduce the basal activity of the receptor in order to achieve low dark noise in the visual system. In contrast, absorption of light triggers rapid isomerization of the retinal, which drives the conversion of the receptor to a fully active conformation. Several specific protein-protein interactions have evolved that maintain the lifetime of the active state in order to increase the sensitivity of this receptor for dim-light vision in vertebrates. In this article, we review the molecular interactions that stabilize rhodopsin in the dark-state and describe the use of solid-state NMR spectroscopy for probing the structural changes that occur upon light-activation. Amino acid conservation provides a guide for those interactions that are common in the class A GPCRs as well as those that are unique to the visual system. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.
PMID: 24183693 [PubMed - as supplied by publisher]
[NMR paper] ?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy.
?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy.
?2 -Adrenergic Receptor Activation by Agonists Studied with (19) F NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 16;
Authors: Horst R, Liu JJ, Stevens RC, Wüthrich K
Abstract
[NMR paper] G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.
Biochem J. 2013 Mar 15;450(3):443-57
Authors: Ding X, Zhao X, Watts A
Abstract
GPCRs (G-protein-coupled receptors) are versatile signalling molecules at the cell surface and make up the largest and most diverse family of membrane receptors in the human genome. They convert a large variety of extracellular stimuli into...
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03-01-2013 09:57 PM
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Biochim Biophys Acta. 2011 Aug 8;
Authors: Mertz B, Struts AV, Feller SE, Brown MF
Abstract
Rhodopsin has served as the primary model for studying G protein-coupled receptors (GPCRs)-the largest group in the human genome, and consequently a primary target for pharmaceutical development. Understanding the functions and activation mechanisms of...
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08-20-2011 03:31 PM
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin [Biophysics and Computational Biology]
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin
Struts, A. V., Salgado, G. F. J., Brown, M. F....
Date: 2011-05-17
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state 2H NMR relaxation allows investigation of light-induced changes in local ps–ns time scale motions of retinal bound to rhodopsin. Site-specific 2H labels were introduced into methyl groups of the...
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05-17-2011 08:40 PM
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Proc Natl Acad Sci U S A. 2011 Apr 28;
Authors: Struts AV, Salgado GF, Brown MF
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state (2)H NMR relaxation...
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04-30-2011 12:36 PM
[NMR paper] Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solutio
Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Related Articles Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3409-13
Authors: Klein-Seetharaman J, Yanamala NV, Javeed F, Reeves PJ, Getmanova EV, Loewen MC, Schwalbe H, Khorana HG
G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the...
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11-24-2010 09:25 PM
[NMR paper] Site-selective screening by NMR spectroscopy with labeled amino acid pairs.
Site-selective screening by NMR spectroscopy with labeled amino acid pairs.
Related Articles Site-selective screening by NMR spectroscopy with labeled amino acid pairs.
J Am Chem Soc. 2002 Mar 20;124(11):2446-7
Authors: Weigelt J, van Dongen M, Uppenberg J, Schultz J, Wikström M
A new method for site-selective screening by NMR is presented. The core of the new method is the dual amino acid sequence specific labeling technique. Amino acid X is labeled with (13)C and amino acid Y is labeled with (15)N. Provided only one XY pair occurs in the...
Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
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