1gmi: Difference between revisions
New page: left|200px<br /> <applet load="1gmi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gmi, resolution 1.7Å" /> '''STRUCTURE OF THE C2 ... |
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==About this Structure== | ==About this Structure== | ||
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]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GMI OCA]]. | 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 12:57, 30 October 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 ... [(full description)]
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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