1gmi: Difference between revisions
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==Overview== | ==Overview== | ||
Protein kinase Cepsilon (PKCepsilon) 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 PKCepsilon, 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 A resolution, respectively. The central feature of the, PKCepsilon-C2 domain structure is an eight-stranded, antiparallel, beta-sandwich with a type II topology similar to that of the C2 domains, from phospholipase C and from novel PKCdelta. Despite the similar, topology, important differences are found ... | Protein kinase Cepsilon (PKCepsilon) 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 PKCepsilon, 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 A resolution, respectively. The central feature of the, PKCepsilon-C2 domain structure is an eight-stranded, antiparallel, beta-sandwich with a type II topology similar to that of the C2 domains, from phospholipase C and from novel PKCdelta. Despite the similar, topology, important differences are found between the structures of C2, domains from PKCs delta and epsilon, suggesting they be considered as, different PKC subclasses. Site-directed mutagenesis experiments and, structural changes in the PKCepsilon-C2 domain from crystals with DCPS or, DCPA indicate, though phospholipids were not visible in these structures, that loops joining strands beta1-beta2 and beta5-beta6 participate in the, binding to anionic membranes. The different behavior in membrane-binding, and activation between PKCepsilon 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 PKCepsilon-C2 domain, with model membranes that retains basic features of the docking of C2, domains from classical, calcium-dependent, PKCs. | ||
==About this Structure== | ==About this Structure== | ||
1GMI is a | 1GMI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GMI OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: x-ray]] | [[Category: x-ray]] | ||
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Revision as of 14:35, 5 November 2007
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STRUCTURE OF THE C2 DOMAIN FROM NOVEL PROTEIN KINASE C EPSILON
OverviewOverview
Protein kinase Cepsilon (PKCepsilon) 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 PKCepsilon, 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 A resolution, respectively. The central feature of the, PKCepsilon-C2 domain structure is an eight-stranded, antiparallel, beta-sandwich with a type II topology similar to that of the C2 domains, from phospholipase C and from novel PKCdelta. Despite the similar, topology, important differences are found between the structures of C2, domains from PKCs delta and epsilon, suggesting they be considered as, different PKC subclasses. Site-directed mutagenesis experiments and, structural changes in the PKCepsilon-C2 domain from crystals with DCPS or, DCPA indicate, though phospholipids were not visible in these structures, that loops joining strands beta1-beta2 and beta5-beta6 participate in the, binding to anionic membranes. The different behavior in membrane-binding, and activation between PKCepsilon 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 PKCepsilon-C2 domain, with model membranes that retains basic features of the docking of C2, domains from classical, calcium-dependent, PKCs.
About this StructureAbout this Structure
1GMI is a Single protein structure of sequence from Rattus rattus with MG as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains., Ochoa WF, Garcia-Garcia J, Fita I, Corbalan-Garcia S, Verdaguer N, Gomez-Fernandez JC, J Mol Biol. 2001 Aug 24;311(4):837-49. PMID:11518534
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