1gmi
|
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 ... [(full description)]
About this StructureAbout this Structure
1GMI is a [Single protein] structure of sequence from [Rattus rattus] with MG as [ligand]. 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
Page seeded by OCA on Mon Oct 29 18:43:37 2007