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000054334 0247_ $$2DOI$$a10.1074/jbc.M603700200
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000054334 084__ $$2WoS$$aBiochemistry & Molecular Biology
000054334 1001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O. H.$$b0$$uFZJ
000054334 245__ $$aTuning of a neuronal calcium sensor
000054334 260__ $$aBethesda, Md.$$bSoc.$$c2006
000054334 300__ $$a37594 - 37602
000054334 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000054334 440_0 $$03091$$aJournal of Biological Chemistry$$v281$$x0021-9258
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000054334 520__ $$aRecoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.
000054334 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000054334 588__ $$aDataset connected to Web of Science, Pubmed
000054334 650_2 $$2MeSH$$aAnimals
000054334 650_2 $$2MeSH$$aBase Sequence
000054334 650_2 $$2MeSH$$aCalcium Signaling: physiology
000054334 650_2 $$2MeSH$$aCattle
000054334 650_2 $$2MeSH$$aCrystallography, X-Ray
000054334 650_2 $$2MeSH$$aDNA Primers: genetics
000054334 650_2 $$2MeSH$$aKinetics
000054334 650_2 $$2MeSH$$aModels, Molecular
000054334 650_2 $$2MeSH$$aMutagenesis, Site-Directed
000054334 650_2 $$2MeSH$$aProtein Structure, Quaternary
000054334 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000054334 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000054334 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000054334 650_2 $$2MeSH$$aRecoverin: chemistry
000054334 650_2 $$2MeSH$$aRecoverin: genetics
000054334 650_2 $$2MeSH$$aRecoverin: metabolism
000054334 650_2 $$2MeSH$$aRod Cell Outer Segment: metabolism
000054334 650_2 $$2MeSH$$aSequence Deletion
000054334 650_2 $$2MeSH$$aSurface Plasmon Resonance
000054334 650_7 $$00$$2NLM Chemicals$$aDNA Primers
000054334 650_7 $$00$$2NLM Chemicals$$aRCV1 protein, Bos taurus
000054334 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000054334 650_7 $$0135844-11-0$$2NLM Chemicals$$aRecoverin
000054334 650_7 $$2WoSType$$aJ
000054334 7001_ $$0P:(DE-HGF)0$$aSenin, I. I.$$b1
000054334 7001_ $$0P:(DE-HGF)0$$aZernii, E.Y.$$b2
000054334 7001_ $$0P:(DE-HGF)0$$aChurumova, V. A.$$b3
000054334 7001_ $$0P:(DE-HGF)0$$aKovaleva, N. A.$$b4
000054334 7001_ $$0P:(DE-HGF)0$$aNazipova, A. A.$$b5
000054334 7001_ $$0P:(DE-HGF)0$$aPermyakov, S.E.$$b6
000054334 7001_ $$0P:(DE-HGF)0$$aPermyakov, E.A.$$b7
000054334 7001_ $$0P:(DE-HGF)0$$aPhilippov, P.P.$$b8
000054334 7001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b9$$uFZJ
000054334 7001_ $$0P:(DE-Juel1)VDB46877$$aKoch, K. W.$$b10$$uFZJ
000054334 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M603700200$$gVol. 281, p. 37594 - 37602$$p37594 - 37602$$q281<37594 - 37602$$tThe @journal of biological chemistry$$v281$$x0021-9258$$y2006
000054334 8567_ $$uhttp://hdl.handle.net/2128/2657$$uhttp://dx.doi.org/10.1074/jbc.M603700200
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000054334 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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