1PKS
STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY
Summary for 1PKS
| Entry DOI | 10.2210/pdb1pks/pdb |
| Descriptor | PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN (1 entity in total) |
| Functional Keywords | phosphotransferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 8977.76 |
| Authors | Koyama, S.,Yu, H.,Dalgarno, D.C.,Shin, T.B.,Zydowsky, L.D.,Schreiber, S.L. (deposition date: 1994-03-07, release date: 1994-05-31, Last modification date: 2024-05-01) |
| Primary citation | Koyama, S.,Yu, H.,Dalgarno, D.C.,Shin, T.B.,Zydowsky, L.D.,Schreiber, S.L. Structure of the PI3K SH3 domain and analysis of the SH3 family. Cell(Cambridge,Mass.), 72:945-952, 1993 Cited by PubMed Abstract: Src homology 3 (SH3) domains, which are found in many proteins involved in intracellular signal transduction, mediate specific protein-protein interactions. The three-dimensional structure of the SH3 domain in the p85 subunit of the phosphatidylinositol 3-kinase (PI3K) has been determined by multidimensional NMR methods. The molecule consists of four short helices, two beta turns, and two antiparallel beta sheets. The beta sheets are highly similar to corresponding regions in the SH3 domain of the tyrosine kinase Src, even though the sequence identity of the two domains is low. There is a unique 15 amino acid insert in PI3K that contains three short helices. There are substantial differences in the identity of the amino acids that make up the receptor site of SH3 domains. The results suggest that while the overall structures of the binding sites in the PI3K and Src SH3 domains are similar, their ligand binding properties may differ. PubMed: 7681364DOI: 10.1016/0092-8674(93)90582-B PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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