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000054914 0247_ $$2pmid$$apmid:17009319
000054914 0247_ $$2DOI$$a10.1002/prot.21158
000054914 0247_ $$2WOS$$aWOS:000242056500018
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000054914 041__ $$aeng
000054914 082__ $$a540
000054914 084__ $$2WoS$$aBiochemistry & Molecular Biology
000054914 084__ $$2WoS$$aBiophysics
000054914 1001_ $$0P:(DE-HGF)0$$aIsin, B.$$b0
000054914 245__ $$aPredisposition of the Three-Dimensional Dark State Structure of Rhodopsin for Functional Conformational Changes
000054914 260__ $$aNew York, NY$$bWiley-Liss$$c2006
000054914 300__ $$a970 - 983
000054914 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000054914 3367_ $$00$$2EndNote$$aJournal Article
000054914 3367_ $$2BibTeX$$aARTICLE
000054914 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000054914 3367_ $$2DRIVER$$aarticle
000054914 440_0 $$016361$$aProteins - Structure Function and Bioinformatics$$v65$$x0887-3585$$y4
000054914 500__ $$aRecord converted from VDB: 12.11.2012
000054914 520__ $$aAs the only member of the family of G-protein-coupled receptors for which atomic coordinates are available, rhodopsin is widely studied for insight into the molecular mechanism of G-protein-coupled receptor activation. The currently available structures refer to the inactive, dark state, of rhodopsin, rather than the light-activated metarhodopsin II (Meta II) state. A model for the Meta II state is proposed here by analyzing elastic network normal modes in conjunction with experimental data. Key mechanical features and interactions broken/formed in the proposed model are found to be consistent with the experimental data. The model is further tested by using a set of Meta II fluorescence decay rates measured to empirically characterize the deactivation of rhodopsin mutants. The model is found to correctly predict 93% of the experimentally observed effects in 119 rhodopsin mutants for which the decay rates and misfolding data have been measured, including a systematic analysis of Cys-->Ser replacements reported here. Based on the detailed comparison between model and experiments, a cooperative activation mechanism is deduced that couples retinal isomerization to concerted changes in conformation, facilitated by the intrinsic dynamics of rhodopsin. A global hinge site is identified near the retinal-binding pocket that ensures the efficient propagation of signals from the central transmembrane region to both cytoplasmic and extracellular ends. The predicted activation mechanism opens the transmembrane helices at the critical G-protein binding cytoplasmic domain. This model provides a detailed, mechanistic description of the activation process, extending experimental observations and yielding new insights for further tests.
000054914 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000054914 588__ $$aDataset connected to Web of Science, Pubmed
000054914 650_2 $$2MeSH$$aAlgorithms
000054914 650_2 $$2MeSH$$aBinding Sites
000054914 650_2 $$2MeSH$$aHydrogen Bonding
000054914 650_2 $$2MeSH$$aIsomerism
000054914 650_2 $$2MeSH$$aLigands
000054914 650_2 $$2MeSH$$aLight
000054914 650_2 $$2MeSH$$aModels, Molecular
000054914 650_2 $$2MeSH$$aNeural Networks (Computer)
000054914 650_2 $$2MeSH$$aPeriodicity
000054914 650_2 $$2MeSH$$aProtein Conformation
000054914 650_2 $$2MeSH$$aReceptors, G-Protein-Coupled: metabolism
000054914 650_2 $$2MeSH$$aRetinaldehyde: chemistry
000054914 650_2 $$2MeSH$$aRetinaldehyde: metabolism
000054914 650_2 $$2MeSH$$aRhodopsin: chemistry
000054914 650_2 $$2MeSH$$aRhodopsin: metabolism
000054914 650_2 $$2MeSH$$aStructure-Activity Relationship
000054914 650_7 $$00$$2NLM Chemicals$$aLigands
000054914 650_7 $$00$$2NLM Chemicals$$aReceptors, G-Protein-Coupled
000054914 650_7 $$0116-31-4$$2NLM Chemicals$$aRetinaldehyde
000054914 650_7 $$060383-01-9$$2NLM Chemicals$$ametarhodopsins
000054914 650_7 $$09009-81-8$$2NLM Chemicals$$aRhodopsin
000054914 650_7 $$2WoSType$$aJ
000054914 65320 $$2Author$$aG-protein-coupled receptors
000054914 65320 $$2Author$$acollective dynamics
000054914 65320 $$2Author$$alight activation
000054914 65320 $$2Author$$aGaussian network model
000054914 65320 $$2Author$$ametarhodopsin II
000054914 65320 $$2Author$$aelastic network
000054914 65320 $$2Author$$aretinal isomerization
000054914 7001_ $$0P:(DE-HGF)0$$aRader, A.J.$$b1
000054914 7001_ $$0P:(DE-HGF)0$$aDhiman, H. K.$$b2
000054914 7001_ $$0P:(DE-Juel1)VDB44599$$aKlein-Seetharaman, J.$$b3$$uFZJ
000054914 7001_ $$0P:(DE-HGF)0$$aBahar, I.$$b4
000054914 773__ $$0PERI:(DE-600)1475032-6$$a10.1002/prot.21158$$gVol. 65, p. 970 - 983$$p970 - 983$$q65<970 - 983$$tProteins$$v65$$x0887-3585$$y2006
000054914 8567_ $$uhttp://dx.doi.org/10.1002/prot.21158
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000054914 9141_ $$y2006
000054914 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000054914 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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