2uwq | pdb_00002uwq

SOLUTION STRUCTURE OF ASPP2 N-TERMINUS

spinqualitylabelsall models 2uwq, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2uwq is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1ycs Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Proteins of the ASPP family bind to p53 and regulate p53-mediated apoptosis. Two family members, ASPP1 and ASPP2, have pro-apoptotic functions while iASPP shows anti-apoptotic responses. However, both the mechanism of enhancement/repression of apoptosis and the molecular basis for their different responses remain unknown. To address the role of the N-termini of pro-apoptotic ASPP proteins, we solved the solution structure of N-ASPP2 (1-83) by NMR spectroscopy. The structure of this domain reveals a beta-Grasp ubiquitin-like fold. Our findings suggest a possible role for the N-termini of ASPP proteins in binding to other proteins in the apoptotic response network and thus mediating their selective pro-apoptotic function. Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.,Tidow H, Andreeva A, Rutherford TJ, Fersht AR J Mol Biol. 2007 Aug 24;371(4):948-58. Epub 2007 May 13. PMID:17594908 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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