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2fk9

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{{STRUCTURE_2fk9| PDB=2fk9 | SCENE= }}
{{STRUCTURE_2fk9| PDB=2fk9 | SCENE= }}
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'''Human protein kinase C, eta'''
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===Human protein kinase C, eta===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16973127}}
==Disease==
==Disease==
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[[Category: Structural genomics consortium]]
[[Category: Structural genomics consortium]]
[[Category: Transferase]]
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Revision as of 09:29, 27 July 2008

Image:2fk9.png

Template:STRUCTURE 2fk9

Contents

Human protein kinase C, eta

Template:ABSTRACT PUBMED 16973127

Disease

Known disease associated with this structure: Cerebral infarction, susceptibility to OMIM:[605437]

About this Structure

2FK9 is a Single protein structure of sequence from Homo sapiens. 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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