Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tidow H, Andreeva A, Rutherford TJ, Fersht AR. Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold. J Mol Biol. 2007 Aug 24;371(4):948-58. Epub 2007 May 13. PMID:17594908 doi:10.1016/j.jmb.2007.05.024
