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000057375 0247_ $$2DOI$$a10.1562/2006-08-25-RA-1014
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000057375 084__ $$2WoS$$aBiochemistry & Molecular Biology
000057375 084__ $$2WoS$$aBiophysics
000057375 1001_ $$0P:(DE-HGF)0$$aSkegro, D.$$b0
000057375 245__ $$aN-terminal and C-terminal Domains of Arrestin Both Contribute in Binding to Rhodopsin (dagger)
000057375 260__ $$aMalden, Mass.$$bWiley-Blackwell$$c2007
000057375 300__ $$a385 - 393
000057375 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000057375 440_0 $$015281$$aPhotochemistry and Photobiology$$v83$$x0031-8655
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000057375 520__ $$aVisual arrestin terminates the signal amplification cascade in photoreceptor cells by blocking the interaction of light activated phosphorylated rhodopsin with the G-protein transducin. Although crystal structures of arrestin and rhodopsin are available, it is still unknown how the complex of the two proteins is formed. To investigate the interaction sites of arrestin with rhodopsin various surface regions of recombinant arrestin were sterically blocked by different numbers of fluorophores (Alexa 633). The binding was recorded by time-resolved light scattering. To accomplish site-specific shielding of protein regions, in a first step all three wild-type cysteines were replaced by alanines. Nevertheless, regarding the magnitude and specificity of rhodopsin binding, the protein is still fully active. In a second step, new cysteines were introduced at selected sites to allow covalent binding of fluorophores. Upon attachment of Alexa 633 to the recombinant cysteines we observed that these bulky labels residing in the concave area of either the N- or the C-terminal domain do not perturb the activity of arrestin. By simultaneously modifying both domains with one Alexa 633 the binding capacity was reduced. The presence of two Alexa 633 molecules in each domain prevented binding of rhodopsin to arrestin. This observation indicates that both concave sites participate in binding.
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000057375 588__ $$aDataset connected to Web of Science, Pubmed
000057375 650_2 $$2MeSH$$aAnimals
000057375 650_2 $$2MeSH$$aArrestin: chemistry
000057375 650_2 $$2MeSH$$aArrestin: genetics
000057375 650_2 $$2MeSH$$aArrestin: metabolism
000057375 650_2 $$2MeSH$$aBase Sequence
000057375 650_2 $$2MeSH$$aBinding Sites
000057375 650_2 $$2MeSH$$aCattle
000057375 650_2 $$2MeSH$$aCysteine: chemistry
000057375 650_2 $$2MeSH$$aDNA Primers: genetics
000057375 650_2 $$2MeSH$$aFluorescent Dyes
000057375 650_2 $$2MeSH$$aModels, Molecular
000057375 650_2 $$2MeSH$$aMutagenesis, Site-Directed
000057375 650_2 $$2MeSH$$aPhotochemistry
000057375 650_2 $$2MeSH$$aProtein Binding
000057375 650_2 $$2MeSH$$aProtein Structure, Tertiary
000057375 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000057375 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000057375 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000057375 650_2 $$2MeSH$$aRhodopsin: metabolism
000057375 650_2 $$2MeSH$$aSignal Transduction
000057375 650_7 $$00$$2NLM Chemicals$$aArrestin
000057375 650_7 $$00$$2NLM Chemicals$$aDNA Primers
000057375 650_7 $$00$$2NLM Chemicals$$aFluorescent Dyes
000057375 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000057375 650_7 $$052-90-4$$2NLM Chemicals$$aCysteine
000057375 650_7 $$09009-81-8$$2NLM Chemicals$$aRhodopsin
000057375 650_7 $$2WoSType$$aJ
000057375 7001_ $$0P:(DE-HGF)0$$aPulvermuller, A.$$b1
000057375 7001_ $$0P:(DE-HGF)0$$aKrafft, B.$$b2
000057375 7001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b3$$uFZJ
000057375 7001_ $$0P:(DE-HGF)0$$aHofmann, K. P.$$b4
000057375 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b5$$uFZJ
000057375 7001_ $$0P:(DE-Juel1)VDB1421$$aSchlesinger, R.$$b6$$uFZJ
000057375 773__ $$0PERI:(DE-600)2048860-9$$a10.1562/2006-08-25-RA-1014$$gVol. 83, p. 385 - 393$$p385 - 393$$q83<385 - 393$$tPhotochemistry and photobiology$$v83$$x0031-8655$$y2007
000057375 8567_ $$uhttp://dx.doi.org/10.1562/2006-08-25-RA-1014
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