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000030298 084__ $$2WoS$$aBiochemistry & Molecular Biology
000030298 1001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O. H.$$b0$$uFZJ
000030298 245__ $$aImpact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin
000030298 260__ $$aBethesda, Md.$$bSoc.$$c2003
000030298 300__ $$a22972 - 22979
000030298 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000030298 440_0 $$03091$$aJournal of Biological Chemistry$$v278$$x0021-9258$$y25
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000030298 520__ $$aRecoverin is a Ca2+-regulated signal transduction modulator found in vertebrate retina that has been shown to undergo dramatic conformational changes upon Ca2+ binding to its two functional EF-hand motifs. To elucidate the differential impact of the N-terminal myristoylation as well as occupation of the two Ca2+ binding sites on recoverin structure and function, we have investigated a non-myristoylated E85Q mutant exhibiting virtually no Ca2+ binding to EF-2. Crystal structures of the mutant protein as well as the non-myristoylated wild-type have been determined. Although the non-myristoylated E85Q mutant does not display any functional activity, its three-dimensional structure in the presence of Ca2+ resembles the myristoylated wild-type with two Ca2+ but is quite dissimilar from the myristoylated E85Q mutant. We conclude that the N-terminal myristoyl modification significantly stabilizes the conformation of the Ca2+-free protein (i.e. the T conformation) during the stepwise transition toward the fully Ca2+-occupied state. On the basis of these observations, a refined model for the role of the myristoyl group as an intrinsic allosteric modulator is proposed.
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000030298 650_2 $$2MeSH$$aAmino Acid Substitution
000030298 650_2 $$2MeSH$$aAnimals
000030298 650_2 $$2MeSH$$aCalcium: metabolism
000030298 650_2 $$2MeSH$$aCalcium-Binding Proteins: chemistry
000030298 650_2 $$2MeSH$$aCalcium-Binding Proteins: metabolism
000030298 650_2 $$2MeSH$$aCattle
000030298 650_2 $$2MeSH$$aCrystallography, X-Ray
000030298 650_2 $$2MeSH$$aEye Proteins
000030298 650_2 $$2MeSH$$aG-Protein-Coupled Receptor Kinase 1
000030298 650_2 $$2MeSH$$aHippocalcin
000030298 650_2 $$2MeSH$$aKinetics
000030298 650_2 $$2MeSH$$aLipoproteins
000030298 650_2 $$2MeSH$$aModels, Molecular
000030298 650_2 $$2MeSH$$aMutagenesis, Site-Directed
000030298 650_2 $$2MeSH$$aMyristic Acid: metabolism
000030298 650_2 $$2MeSH$$aNerve Tissue Proteins
000030298 650_2 $$2MeSH$$aProtein Binding
000030298 650_2 $$2MeSH$$aProtein Conformation
000030298 650_2 $$2MeSH$$aProtein Kinases: metabolism
000030298 650_2 $$2MeSH$$aProtein Structure, Secondary
000030298 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000030298 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000030298 650_2 $$2MeSH$$aRecoverin
000030298 650_2 $$2MeSH$$aRod Cell Outer Segment: metabolism
000030298 650_2 $$2MeSH$$aTumor Markers, Biological: chemistry
000030298 650_2 $$2MeSH$$aTumor Markers, Biological: metabolism
000030298 650_7 $$00$$2NLM Chemicals$$aCalcium-Binding Proteins
000030298 650_7 $$00$$2NLM Chemicals$$aEye Proteins
000030298 650_7 $$00$$2NLM Chemicals$$aLipoproteins
000030298 650_7 $$00$$2NLM Chemicals$$aNerve Tissue Proteins
000030298 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000030298 650_7 $$00$$2NLM Chemicals$$aTumor Markers, Biological
000030298 650_7 $$0135844-11-0$$2NLM Chemicals$$aRecoverin
000030298 650_7 $$0149223-81-4$$2NLM Chemicals$$aHippocalcin
000030298 650_7 $$0544-63-8$$2NLM Chemicals$$aMyristic Acid
000030298 650_7 $$07440-70-2$$2NLM Chemicals$$aCalcium
000030298 650_7 $$0EC 2.7.-$$2NLM Chemicals$$aProtein Kinases
000030298 650_7 $$0EC 2.7.11.14$$2NLM Chemicals$$aG-Protein-Coupled Receptor Kinase 1
000030298 650_7 $$2WoSType$$aJ
000030298 7001_ $$0P:(DE-HGF)0$$aSenin, I. I.$$b1
000030298 7001_ $$0P:(DE-HGF)0$$aPhilippov, P. P.$$b2
000030298 7001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b3$$uFZJ
000030298 7001_ $$0P:(DE-Juel1)VDB789$$aKoch, K.-W.$$b4$$uFZJ
000030298 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M300447200$$gVol. 278, p. 22972 - 22979$$p22972 - 22979$$q278<22972 - 22979$$tThe @journal of biological chemistry$$v278$$x0021-9258$$y2003
000030298 8567_ $$uhttp://hdl.handle.net/2128/2643$$uhttp://dx.doi.org/10.1074/jbc.M300447200
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000030298 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x1
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