Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites.
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.
Littler
Dene R
DR
Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ont., Canada M5G 1L5.
Walker
John R
JR
She
Yi-Min
YM
Finerty
Patrick J
PJ
Newman
Elena M
EM
Dhe-Paganon
Sirano
S
D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D011493:Protein Kinase C / Q000737:chemistry* / Q000648:ultrastructure*; D017434:Protein Structure, Tertiary
C081975:protein kinase C eta; D011493:Protein Kinase C