2fk9
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Human protein kinase C, eta
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. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 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
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- Homo sapiens
- Non-specific serine/threonine protein kinase
- Single protein
- Arrowsmith, C.
- Bochkarev, A.
- Dhe-Paganon, S.
- Edwards, A.
- Jr., P J.Finerty.
- Littler, D R.
- MacKenzie, F.
- Newman, E M.
- SGC, Structural Genomics Consortium.
- Sundstrom, M.
- Walker, J R.
- Weigelt, J.
- Atp-binding
- Diacylglycerol binding
- Kinase
- Metal-binding
- Nucleotide-binding
- Serine/threonine-protein kinase
- Sgc
- Structural genomics
- Structural genomics consortium
- Transferase