2fk9

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(New page: 200px<br /><applet load="2fk9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fk9, resolution 1.75&Aring;" /> '''Human protein kinase...)
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Revision as of 17:38, 29 January 2008


2fk9, resolution 1.75Å

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Human protein kinase C, eta

Overview

Protein kinase C eta (PKCeta) is one of several PKC isoforms found in, humans. It is a novel PKC isoform in that it is activated by, diacylglycerol and anionic phospholipids but not calcium. The crystal, structure of the PKCeta-C2 domain, which is thought to mediate anionic, phospholipid sensing in the protein, was determined at 1.75 A resolution., The structure is similar to that of the PKC epsilon C2 domain but with, significant variations at the putative lipid-binding site. Two serine, residues within PKC eta were identified in vitro as potential, autophosphorylation sites. In the unphosphorylated structure both serines, line the putative lipid-binding site and may therefore play a role in the, lipid-regulation of the kinase.

About this Structure

2FK9 is a Single protein structure of sequence from Homo sapiens. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites., Littler DR, Walker JR, She YM, Finerty PJ Jr, Newman EM, Dhe-Paganon S, Biochem Biophys Res Commun. 2006 Nov 3;349(4):1182-9. Epub 2006 Sep 5. PMID:16973127

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