2b3r
From Proteopedia
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Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2
Overview
Phosphatidylinositide (PtdIns) 3-kinase catalyzes the addition of a, phosphate group to the 3'-position of phosphatidyl inositol. Accumulated, evidence shows that PtdIns 3-kinase can provide a critical signal for cell, proliferation, cell survival, membrane trafficking, glucose transport, and, membrane ruffling. Mammalian PtdIns 3-kinases are divided into three, classes based on structure and substrate specificity. A unique, characteristic of class II PtdIns 3-kinases is the presence of both a phox, homolog domain and a C2 domain at the C terminus. The biological function, of the C2 domain of the class II PtdIns 3-kinases remains to be, determined. We have determined the crystal structure of the mCPK-C2, domain, which is the first three-dimensional structural model of a C2, domain of class II PtdIns 3-kinases. Structural studies reveal that the, mCPK-C2 domain has a typical anti-parallel beta-sandwich fold. Scrutiny of, the surface of this C2 domain has identified three small, shallow, sulfate-binding sites. On the basis of the structural features of these, sulfate-binding sites, we have studied the lipid binding properties of the, mCPK-C2 domain by site-directed mutagenesis. Our results show that this C2, domain binds specifically to PtdIns(3,4)P(2) and PtdIns(4,5)P(2) and that, three lysine residues at SBS I site, Lys-1420, Lys-1432, and Lys-1434, are, responsible for the phospholipid binding affinity.
About this Structure
2B3R is a Single protein structure of sequence from Mus musculus with SO4 as ligand. Active as Phosphatidylinositol-4-phosphate 3-kinase, with EC number 2.7.1.154 Full crystallographic information is available from OCA.
Reference
Crystal structure of the C2 domain of class II phosphatidylinositide 3-kinase C2alpha., Liu L, Song X, He D, Komma C, Kita A, Virbasius JV, Huang G, Bellamy HD, Miki K, Czech MP, Zhou GW, J Biol Chem. 2006 Feb 17;281(7):4254-60. Epub 2005 Dec 7. PMID:16338929
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