2fk9: Difference between revisions

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[[Image:2fk9.gif|left|200px]]
{{Seed}}
[[Image:2fk9.png|left|200px]]


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{{STRUCTURE_2fk9|  PDB=2fk9  |  SCENE=  }}  
{{STRUCTURE_2fk9|  PDB=2fk9  |  SCENE=  }}  


'''Human protein kinase C, eta'''
===Human protein kinase C, eta===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_16973127}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16973127}}


==Disease==
==Disease==
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[[Category: Structural genomics consortium]]
[[Category: Structural genomics consortium]]
[[Category: Transferase]]
[[Category: Transferase]]
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