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1YCSP53-53BP2 COMPLEXStructure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2.author(s): Gorina, S., Pavletich, N.P. The structure of the complex shows that the 53BP2 binding site on the p53 core domain consists of evolutionarily conserved regions that are frequently mutated in cancer and that it overlaps the site of DNA binding. The six most frequently observed p53 mutations disrupt 53BP2 binding in vitro. The structure provides evidence that the 53BP2-p53 complex forms in vivo and may have a critical role in the p53 pathway of tumor suppression. Citation 1YCS (PDB) |
1YCQXENOPUS LAEVIS MDM2 BOUND TO THE TRANSACTIVATION DOMAIN OF HUMAN P53Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain.author(s): Kussie, P.H., Pavletich, N.P. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors. Citation (PubMed) 1YCQ (PDB) Back to Table |