2FK9

Human protein kinase C, eta

Summary for 2FK9

• Entry DOI: 10.2210/pdb2fk9/pdb
• Descriptor: protein kinase C, eta type (2 entities in total)
• Functional Keywords: atp-binding, kinase, metal-binding, nucleotide-binding, diacylglycerol binding, serine/threonine-protein kinase, transferase, structural genomics, structural genomics consortium, sgc
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 17501.67

Authors

Walker, J.R.,Littler, D.R.,Finerty Jr., P.J.,MacKenzie, F.,Newman, E.M.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.,Edwards, A.,Bochkarev, A.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (deposition date: 2006-01-04, release date: 2006-01-17, Last modification date: 2023-08-30)

Primary citation

Littler, D.R.,Walker, J.R.,She, Y.M.,Finerty, P.J.,Newman, E.M.,Dhe-Paganon, S.
Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites.
Biochem.Biophys.Res.Commun., 349:1182-1189, 2006

PubMed 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.

PubMed: 16973127
DOI: 10.1016/j.bbrc.2006.08.160

Experimental method

X-RAY DIFFRACTION (1.75 Å)