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000007146 0247_ $$2pmid$$apmid:19835414
000007146 0247_ $$2DOI$$a10.1021/bi900544p
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000007146 084__ $$2WoS$$aBiochemistry & Molecular Biology
000007146 1001_ $$0P:(DE-Juel1)VDB89238$$aFeuerstein, S.E.$$b0$$uFZJ
000007146 245__ $$aHelix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin
000007146 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2009
000007146 300__ $$a10733  -10742
000007146 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000007146 440_0 $$0798$$aBiochemistry$$v48$$x0006-2960$$y45
000007146 500__ $$aThis work was supported by grants from the Deutsche Forschungsgemeinschaft (DFG) to B.W.K. (Ko 2143/3), AR (Pu 186/3), and O.P. E. (Er 294/1).
000007146 520__ $$aBinding of arrestin to photoactivated phosphorylated rhodopsin terminates the amplification of visual signals in photoreceptor cells. Currently, there is no crystal structure of a rhodopsin-arrestin complex available, although structures of unbound rhodopsin and arrestin have been determined. High-affinity receptor binding is dependent on distinct arrestin sites responsible for recognition of rhodopsin activation and phosphorylation. The loop connecting beta-strands V and VI in rod arrestin has been implicated in the recognition of active rhodopsin. We report the structure of receptor-bound arrestin peptide Arr(67-77) mimicking this loop based on solution NMR data. The peptide binds photoactivated rhodopsin in the unphosphorylated and phosphorylated form with similar affinities and stabilizes the metarhodopsin II photointermediate. A largely alpha-helical conformation of the receptor-bound peptide is observed.
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000007146 650_2 $$2MeSH$$aArrestin: chemistry
000007146 650_2 $$2MeSH$$aModels, Molecular
000007146 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000007146 650_2 $$2MeSH$$aPhotochemistry
000007146 650_2 $$2MeSH$$aProtein Conformation
000007146 650_2 $$2MeSH$$aRhodopsin: chemistry
000007146 650_7 $$00$$2NLM Chemicals$$aArrestin
000007146 650_7 $$09009-81-8$$2NLM Chemicals$$aRhodopsin
000007146 650_7 $$2WoSType$$aJ
000007146 7001_ $$0P:(DE-HGF)0$$aPulvermüller, A.$$b1
000007146 7001_ $$0P:(DE-Juel1)VDB57647$$aHartmann, R.$$b2$$uFZJ
000007146 7001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b3$$uFZJ
000007146 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b4$$uFZJ
000007146 7001_ $$0P:(DE-HGF)0$$aHenklein, P.$$b5
000007146 7001_ $$0P:(DE-HGF)0$$aErnst, O.P.$$b6
000007146 7001_ $$0P:(DE-HGF)0$$aHeck, M.$$b7
000007146 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b8$$uFZJ
000007146 7001_ $$0P:(DE-Juel1)132009$$aKoenig, B. W.$$b9$$uFZJ
000007146 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi900544p$$gVol. 48, p. 10733  -10742$$p10733  -10742$$q48<10733  -10742$$tBiochemistry$$v48$$x0006-2960$$y2009
000007146 8567_ $$uhttp://dx.doi.org/10.1021/bi900544p
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