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000111980 0247_ $$2DOI$$a10.1016/j.jmb.2012.01.028
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000111980 041__ $$aeng
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000111980 084__ $$2WoS$$aBiochemistry & Molecular Biology
000111980 1001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b0$$uFZJ
000111980 245__ $$aCrystal structure of p44, a constitutively active splice variant of visual arrestin
000111980 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2012
000111980 300__ $$a611 - 618
000111980 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000111980 440_0 $$03552$$aJournal of Molecular Biology$$v416$$x0022-2836$$y5
000111980 500__ $$aWe are grateful to the beamline scientists at the European Synchrotron Radiation Facility (Grenoble, France) for providing assistance with the use of beamline ID14-4. We thank Oliver H. Weiergraber for comments on the manuscript, Bianca Krafft for generating the p44 clone in S. cerevisiae, and Dieter Willbold and the Russian Group ONEXIM (GB) for generous support.
000111980 520__ $$aVisual arrestin specifically binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. In contrast, the p44 splice variant can terminate phototransduction by binding to nonphosphorylated light-activated rhodopsin. Here we report the crystal structure of bovine p44 at a resolution of 1.85 Å. Compared to native arrestin, the p44 structure reveals significant differences in regions crucial for receptor binding, namely flexible loop V-VI and polar core regions. Additionally, electrostatic potential is remarkably positive on the N-domain and the C-domain. The p44 structure represents an active conformation that serves as a model to explain the 'constitutive activity' found in arrestin variants.
000111980 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000111980 536__ $$0G:(DE-Juel1)FUEK409$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x1
000111980 588__ $$aDataset connected to Web of Science, Pubmed
000111980 65320 $$2Author$$aarrestin
000111980 65320 $$2Author$$asplice variant
000111980 65320 $$2Author$$ap44
000111980 65320 $$2Author$$arhodopsin
000111980 65320 $$2Author$$aphotoreceptor
000111980 650_2 $$2MeSH$$aAnimals
000111980 650_2 $$2MeSH$$aArrestin: chemistry
000111980 650_2 $$2MeSH$$aArrestin: genetics
000111980 650_2 $$2MeSH$$aArrestin: metabolism
000111980 650_2 $$2MeSH$$aCattle
000111980 650_2 $$2MeSH$$aCrystallography, X-Ray: methods
000111980 650_2 $$2MeSH$$aGenetic Variation
000111980 650_2 $$2MeSH$$aLight Signal Transduction
000111980 650_2 $$2MeSH$$aModels, Molecular
000111980 650_2 $$2MeSH$$aPhosphorylation
000111980 650_2 $$2MeSH$$aProtein Binding
000111980 650_2 $$2MeSH$$aProtein Structure, Tertiary: genetics
000111980 650_2 $$2MeSH$$aRNA Splicing
000111980 650_2 $$2MeSH$$aRhodopsin: metabolism
000111980 650_2 $$2MeSH$$aStatic Electricity
000111980 650_7 $$00$$2NLM Chemicals$$aArrestin
000111980 650_7 $$09009-81-8$$2NLM Chemicals$$aRhodopsin
000111980 650_7 $$2WoSType$$aJ
000111980 7001_ $$0P:(DE-Juel1)VDB31224$$aCousin, A.$$b1$$uFZJ
000111980 7001_ $$0P:(DE-Juel1)VDB104857$$aWeirauch, M.$$b2$$uFZJ
000111980 7001_ $$0P:(DE-HGF)0$$aSchlesinger, R.$$b3
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000111980 7001_ $$0P:(DE-Juel1)VDB58515$$aBatra-Safferling, R.$$b5$$uFZJ
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000111980 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2012.01.028
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