000136533 001__ 136533
000136533 005__ 20210129211846.0
000136533 0247_ $$2DOI$$a10.1515/BC.2005.034
000136533 0247_ $$2WOS$$aWOS:000228131400011
000136533 0247_ $$2Handle$$a2128/18397
000136533 037__ $$aFZJ-2013-03329
000136533 041__ $$aEnglish
000136533 082__ $$a540
000136533 1001_ $$0P:(DE-HGF)0$$aKomolov, K. E.$$b0$$eCorresponding author
000136533 245__ $$aOne of the Ca(2+) binding sites of recoverin exclusively controls interaction with rhodopsin kinase
000136533 260__ $$aBerlin [u.a.]$$bde Gruyter$$c2005
000136533 3367_ $$2DRIVER$$aarticle
000136533 3367_ $$2DataCite$$aOutput Types/Journal article
000136533 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1374675177_27988
000136533 3367_ $$2BibTeX$$aARTICLE
000136533 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000136533 3367_ $$00$$2EndNote$$aJournal Article
000136533 520__ $$aRecoverin is a neuronal calcium sensor protein that controls the activity of rhodopsin kinase in a Ca(2+)-dependent manner. Mutations in the EF-hand Ca2+ binding sites are valuable tools for investigating the functional properties of recoverin. In the recoverin mutant E121Q (Rec E121Q ) the high-affinity Ca2+ binding site is disabled. The non-myristoylated form of Rec E121Q binds one Ca2+ via its second Ca(2+)-binding site (EF-hand 2), whereas the myristoylated variant does not bind Ca2+ at all. Binding of Ca2+ to non-myristoylated Rec E121Q apparently triggers exposure of apolar side chains, allowing for association with hydrophobic matrices. Likewise, an interaction surface for the recoverin target rhodopsin kinase is constituted upon Ca2+ binding to the non-acylated mutant. Structural changes resulting from Ca(2+)-occupation of EF-hand 2 in myristoylated and non-myristoylated recoverin variants are discussed in terms of critical conditions required for biological activity.
000136533 536__ $$0G:(DE-HGF)POF2-452$$a452 - Structural Biology (POF2-452)$$cPOF2-452$$fPOF II$$x0
000136533 7001_ $$0P:(DE-HGF)0$$aZinchenko, D. V.$$b1
000136533 7001_ $$0P:(DE-HGF)0$$aChurumova, V. A.$$b2
000136533 7001_ $$0P:(DE-HGF)0$$aVaganova, S. A.$$b3
000136533 7001_ $$0P:(DE-Juel1)131988$$aWeiergräber, Oliver H.$$b4$$ufzj
000136533 7001_ $$0P:(DE-HGF)0$$aSenin, I. I.$$b5
000136533 7001_ $$0P:(DE-HGF)0$$aPhilippov, P. P.$$b6
000136533 7001_ $$0P:(DE-HGF)0$$aKoch, K. W.$$b7
000136533 773__ $$0PERI:(DE-600)1466062-3$$p285-286$$tBiological chemistry$$v386$$x1431-6730
000136533 8564_ $$uhttp://www.ncbi.nlm.nih.gov/pubmed/15843174
000136533 8564_ $$uhttps://juser.fz-juelich.de/record/136533/files/%5BBiological%20Chemistry%5D%20One%20of%20the%20Ca2%20binding%20sites%20of%20recoverin%20exclusively%20controls%20interaction%20with%20rhodopsin%20kinase.pdf$$yOpenAccess
000136533 8564_ $$uhttps://juser.fz-juelich.de/record/136533/files/%5BBiological%20Chemistry%5D%20One%20of%20the%20Ca2%20binding%20sites%20of%20recoverin%20exclusively%20controls%20interaction%20with%20rhodopsin%20kinase.gif?subformat=icon$$xicon$$yOpenAccess
000136533 8564_ $$uhttps://juser.fz-juelich.de/record/136533/files/%5BBiological%20Chemistry%5D%20One%20of%20the%20Ca2%20binding%20sites%20of%20recoverin%20exclusively%20controls%20interaction%20with%20rhodopsin%20kinase.jpg?subformat=icon-180$$xicon-180$$yOpenAccess
000136533 8564_ $$uhttps://juser.fz-juelich.de/record/136533/files/%5BBiological%20Chemistry%5D%20One%20of%20the%20Ca2%20binding%20sites%20of%20recoverin%20exclusively%20controls%20interaction%20with%20rhodopsin%20kinase.jpg?subformat=icon-700$$xicon-700$$yOpenAccess
000136533 909CO $$ooai:juser.fz-juelich.de:136533$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire
000136533 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131988$$aForschungszentrum Jülich GmbH$$b4$$kFZJ
000136533 9131_ $$0G:(DE-HGF)POF2-452$$1G:(DE-HGF)POF2-450$$2G:(DE-HGF)POF2-400$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$aDE-HGF$$bSchlüsseltechnologien$$lBioSoft$$vStructural Biology$$x0
000136533 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000136533 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000136533 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000136533 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000136533 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000136533 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000136533 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000136533 915__ $$0StatID:(DE-HGF)0010$$2StatID$$aJCR/ISI refereed
000136533 915__ $$0StatID:(DE-HGF)0410$$2StatID$$aAllianz-Lizenz
000136533 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000136533 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000136533 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000136533 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000136533 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000136533 920__ $$lyes
000136533 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000136533 9801_ $$aFullTexts
000136533 980__ $$ajournal
000136533 980__ $$aVDB
000136533 980__ $$aUNRESTRICTED
000136533 980__ $$aI:(DE-Juel1)ICS-6-20110106
000136533 981__ $$aI:(DE-Juel1)IBI-7-20200312