2PNB
STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE
Summary for 2PNB
| Entry DOI | 10.2210/pdb2pnb/pdb |
| Descriptor | PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT N-TERMINAL SH2 DOMAIN (1 entity in total) |
| Functional Keywords | signalling protein |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 12147.63 |
| Authors | Booker, G.W.,Breeze, A.L.,Downing, A.K.,Panayotou, G.,Gout, I.,Waterfield, M.D.,Campbell, I.D. (deposition date: 1992-06-30, release date: 1994-01-31, Last modification date: 2024-05-01) |
| Primary citation | Booker, G.W.,Breeze, A.L.,Downing, A.K.,Panayotou, G.,Gout, I.,Waterfield, M.D.,Campbell, I.D. Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase. Nature, 358:684-687, 1992 Cited by PubMed Abstract: 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. PubMed: 1323062DOI: 10.1038/358684a0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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