2fk9
From Proteopedia
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Human protein kinase C, eta
Overview
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 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.
Reference
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 Tue Jan 29 19:38:31 2008
Categories: 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
