2pnb
From Proteopedia
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STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE
Overview
Receptor protein-tyrosine kinases, through phosphorylation of specific, tyrosine residues, generate high-affinity binding sites which direct, assembly of multienzyme signalling complexes. Many of these signalling, proteins, including phospholipase C gamma, GTPase-activating protein and, phosphatidylinositol-3-OH kinase, contain src-homology 2 (SH2) domains, which bind with high affinity and specificity to tyrosine-phosphorylated, sequences. The critical role played by SH2 domains in signalling has been, highlighted by recent studies showing that mutation of specific, phosphorylation sites on the platelet-derived growth factor receptor, impair its association with phosphatidylinositol-3-OH kinase, preventing, growth factor-induced mitogenesis. Here we report the solution structure, of an isolated SH2 domain from the 85K regulatory subunit of, phosphatidylinositol-3-OH kinase, determined using multidimensional, nuclear magnetic resonance spectroscopy. The structure is characterized by, a central region of beta-sheet flanked by two alpha-helices, with a highly, flexible loop close to functionally important residues previously, identified by site-directed mutagenesis.
About this Structure
2PNB is a Single protein structure of sequence from Bos taurus. Active as Phosphatidylinositol 3-kinase, with EC number 2.7.1.137 Full crystallographic information is available from OCA.
Reference
Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase., Booker GW, Breeze AL, Downing AK, Panayotou G, Gout I, Waterfield MD, Campbell ID, Nature. 1992 Aug 20;358(6388):684-7. PMID:1323062
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