1gmi: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gmi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GMI FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gmi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GMI FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gmi RCSB], [http://www.ebi.ac.uk/pdbsum/1gmi PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gmi RCSB], [http://www.ebi.ac.uk/pdbsum/1gmi PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Rattus rattus]] | [[Category: Rattus rattus]] | ||
[[Category: Corbalan-Garcia, S | [[Category: Corbalan-Garcia, S]] | ||
[[Category: Fita, I | [[Category: Fita, I]] | ||
[[Category: Garcia-Garcia, J | [[Category: Garcia-Garcia, J]] | ||
[[Category: Gomez-Fernandez, J C | [[Category: Gomez-Fernandez, J C]] | ||
[[Category: Ochoa, W F | [[Category: Ochoa, W F]] | ||
[[Category: Verdaguer, N | [[Category: Verdaguer, N]] | ||
[[Category: C2 domain]] | [[Category: C2 domain]] | ||
[[Category: Kinase]] | [[Category: Kinase]] | ||
[[Category: Phospholipid]] | [[Category: Phospholipid]] | ||
[[Category: Pkc]] | [[Category: Pkc]] | ||
[[Category: Pkc epsilon | [[Category: Pkc epsilon]] | ||
Revision as of 22:06, 22 December 2014
STRUCTURE OF THE C2 DOMAIN FROM NOVEL PROTEIN KINASE C EPSILONSTRUCTURE OF THE C2 DOMAIN FROM NOVEL PROTEIN KINASE C EPSILON
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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