2xwc

Crystal structure of the DNA binding domain of human TP73 refined at 1.8 A resolution

spinqualitylabelsall models 2xwc, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xwc is a 1 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 2xip. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, TAM, ZN Related: 1dxs, 2wqj, 2wqi, 1cok, 2wtt Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [P73_HUMAN] Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. Publication Abstract from PubMed Tumor suppressors p53, p63 and p73 comprise a family of stress-responsive transcription factors with distinct functions in development and tumor suppression. Most human cancers lose p53 function, yet all three proteins are capable of inducing apoptosis or cellular senescence. Mechanisms are therefore under investigation to activate p73-dependent apoptosis in p53-deficient cancer cells. Significantly, the DNA-binding domain (DBD) of p73 escapes viral oncoproteins and displays an enhanced thermal stability. To further understand the variant features of p73, we solved the high-resolution crystal structure of the p73 DBD as well as its complex with the ankyrin repeat and SH3 domains of the pro-apoptotic factor ASPP2. The p73 structure exhibits the same conserved architecture as p53 but displays a divergent L2 loop, a known site of protein-protein interaction. The loop in p73 is changed by a two-residue insertion that also induces repacking around the site of the p53 mutational hotspot R175. Importantly, the binding of ASPP2 is preserved by conformational changes in both the ankyrin repeat and SH3 domains. These results further highlight the structural variation that impacts p53 family interactions within the p53 interactome. Structural Basis for ASPP2 Recognition by the Tumor Suppressor p73.,Canning P, von Delft F, Bullock AN J Mol Biol. 2012 Aug 20. pii: S0022-2836(12)00648-1. doi:, 10.1016/j.jmb.2012.08.005. PMID:22917970 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also P73

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