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dc.contributor.authorOchoa, Wendy F.-
dc.contributor.authorGarcía-García, Josefa-
dc.contributor.authorFita, Ignacio-
dc.contributor.authorCorbalán-García, Senena-
dc.contributor.authorVerdaguer, Núria-
dc.contributor.authorGómez-Fernández, Juan C.-
dc.date.accessioned2015-02-06T10:54:24Z-
dc.date.available2015-02-06T10:54:24Z-
dc.date.issued2001-08-24-
dc.identifierdoi: 10.1006/jmbi.2001.4910-
dc.identifierissn: 0022-2836-
dc.identifier.citationJournal of Molecular Biology 311(4): 837-849 (2001)-
dc.identifier.urihttp://hdl.handle.net/10261/110330-
dc.description.abstractProtein kinase Cε (PKCε) is a member of the novel PKCs which are activated by acidic phospholipids, diacylglycerol and phorbol esters, but lack the calcium dependence of classical PKC isotypes. The crystal structures of the C2 domain of PKCε, crystallized both in the absence and in the presence of the two acidic phospholipids, 1,2-dicaproyl-sn-phosphatidyl-L-serine (DCPS) and 1,2-dicaproyl-sn-phosphatidic acid (DCPA), have now been determined at 2.1, 1.7 and 2.8 Å resolution, respectively. The central feature of the PKCε-C2 domain structure is an eight-stranded, antiparallel, β-sandwich with a type II topology similar to that of the C2 domains from phospholipase C and from novel PKCδ. Despite the similar topology, important differences are found between the structures of C2 domains from PKCs δ and ε, suggesting they be considered as different PKC subclasses. Site-directed mutagenesis experiments and structural changes in the PKCε-C2 domain from crystals with DCPS or DCPA indicate, though phospholipids were not visible in these structures, that loops joining strands β1-β2 and β5-β6 participate in the binding to anionic membranes. The different behavior in membrane-binding and activation between PKCε and classical PKCs appears to originate in localized structural changes, which include a major reorganization of the region corresponding to the calcium binding pocket in classical PKCs. A mechanism is proposed for the interaction of the PKCε-C2 domain with model membranes that retains basic features of the docking of C2 domains from classical, calcium-dependent, PKCs. © 2001 Academic Press.-
dc.description.sponsorshipThis research was supported by grant 1FD97-1558 from DGESIC (Spain). Research at the IBMB was also supported by grant PB95-0218, and research at Universidad de Murcia by grant PB98-0389 from DGESIC (Spain). W.F.O. and J.G.G. are the recipients of fellowships from Ministerio de Educación y Cultura (Spain).-
dc.publisherAcademic Press-
dc.rightsclosedAccess-
dc.subjectNovel protein kinase C-
dc.subjectPhosphatidic acid-
dc.subjectPhosphatidylserine-
dc.subjectX-ray structure-
dc.subjectC2 domain-
dc.titleStructure of the C2 domain from novel protein kinase Cε. A membrane binding model for Ca2+-independent C2 domains-
dc.typeartículo-
dc.identifier.doi10.1006/jmbi.2001.4910-
dc.relation.publisherversionhttp://dx.doi.org/10.1006/jmbi.2001.4910-
dc.date.updated2015-02-06T10:54:25Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
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