2RD0
Structure of a human p110alpha/p85alpha complex
Summary for 2RD0
| Entry DOI | 10.2210/pdb2rd0/pdb |
| Descriptor | Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform, Phosphatidylinositol 3-kinase regulatory subunit alpha (2 entities in total) |
| Functional Keywords | disease mutation, kinase, oncogene, transferase, host-virus interaction, phosphorylation, sh2 domain, sh3 domain, transferase-oncoprotein complex, transferase/oncoprotein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 161489.54 |
| Authors | Huang, C.,Gabelli, S.B.,Amzel, L.M. (deposition date: 2007-09-20, release date: 2007-12-25, Last modification date: 2024-02-21) |
| Primary citation | Huang, C.H.,Mandelker, D.,Schmidt-Kittler, O.,Samuels, Y.,Velculescu, V.E.,Kinzler, K.W.,Vogelstein, B.,Gabelli, S.B.,Amzel, L.M. The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations. Science, 318:1744-1748, 2007 Cited by PubMed Abstract: PIK3CA, one of the two most frequently mutated oncogenes in human tumors, codes for p110alpha, the catalytic subunit of a phosphatidylinositol 3-kinase, isoform alpha (PI3Kalpha, p110alpha/p85). Here, we report a 3.0 angstrom resolution structure of a complex between p110alpha and a polypeptide containing the p110alpha-binding domains of p85alpha, a protein required for its enzymatic activity. The structure shows that many of the mutations occur at residues lying at the interfaces between p110alpha and p85alpha or between the kinase domain of p110alpha and other domains within the catalytic subunit. Disruptions of these interactions are likely to affect the regulation of kinase activity by p85 or the catalytic activity of the enzyme, respectively. In addition to providing new insights about the structure of PI3Kalpha, these results suggest specific mechanisms for the effect of oncogenic mutations in p110alpha and p85alpha. PubMed: 18079394DOI: 10.1126/science.1150799 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.05 Å) |
Structure validation
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