Structure of Human Protein Kinase C Eta (Pkceta) C2 Domain and Identification of Phosphorylation Sites.
From: Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ont., Canada M5G 1L5.
Biochemical and biophysical research communications
- Publish Date: Nov 2006
- ISSN: 0006-291X
- Volume: 349
- Issue: 4
- Pages: 1182-9
- Medium: Print
- Language: English
- Citation (JAMA): Littler Dene R, Walker John R, She Yi-Min, et al. Structure of Human Protein Kinase C Eta (Pkceta) C2 Domain and Identification of Phosphorylation Sites.. Biochem. Biophys. Res. Commun. Nov 2006;349:1182-9
Abstract
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.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Computer Simulation, Models, Chemical, Models, Molecular, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Conformation, Protein Kinase C, Protein Structure, Tertiary
Check for Full Text / PubMed Unique Identifier (PMID): 16973127
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