1PNJ
SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE
Summary for 1PNJ
| Entry DOI | 10.2210/pdb1pnj/pdb |
| Descriptor | PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN (1 entity in total) |
| Functional Keywords | phosphotransferase |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 9649.58 |
| Authors | Booker, G.W.,Gout, I.,Downing, A.K.,Driscoll, P.C.,Boyd, J.,Waterfield, M.D.,Campbell, I.D. (deposition date: 1993-07-19, release date: 1993-10-31, Last modification date: 2024-05-01) |
| Primary citation | Booker, G.W.,Gout, I.,Downing, A.K.,Driscoll, P.C.,Boyd, J.,Waterfield, M.D.,Campbell, I.D. Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase. Cell(Cambridge,Mass.), 73:813-822, 1993 Cited by PubMed Abstract: SH3 domains are found in proteins associated with receptor tyrosine kinase signal transduction complexes. The solution structure of the SH3 domain of the 85 kd regulatory subunit of phosphatidylinositol 3-kinase is shown to be a compact beta barrel consisting of five beta strands arranged in two beta sheets of three and two strands. The structure is similar to that of chicken brain alpha spectrin but represents a distinct class of SH3 domain, with an insertion between the second and third beta strands that may influence binding specificity. 1H chemical shift changes induced by complex formation with a synthetic peptide derived from the SH3-binding protein dynamin, together with amino acid sequence comparisons, suggest that the ligand-binding site consists of a hydrophobic surface flanked by two charged loops. PubMed: 7684655DOI: 10.1016/0092-8674(93)90259-S PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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