2fk9
Human protein kinase C, eta
| |||||||
, resolution 1.75Å | |||||||
---|---|---|---|---|---|---|---|
Gene: | PRKCH (Homo sapiens) | ||||||
Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
OverviewOverview
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 StructureAbout this Structure
2FK9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Mar 20 16:53:26 2008