2UWQ
Solution structure of ASPP2 N-terminus
Summary for 2UWQ
| Entry DOI | 10.2210/pdb2uwq/pdb |
| Related | 1YCS |
| Descriptor | APOPTOSIS-STIMULATING OF P53 PROTEIN 2 (1 entity in total) |
| Functional Keywords | aspp2, ubiquitin-like, sh3-domain, apoptosis, cell cycle, ank repeat, sh3-binding |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm, perinuclear region: Q13625 |
| Total number of polymer chains | 1 |
| Total formula weight | 9976.22 |
| Authors | Tidow, H.,Rutherford, T.J.,Andreeva, A.,Fersht, A.R. (deposition date: 2007-03-22, release date: 2007-07-10, Last modification date: 2024-05-15) |
| Primary citation | Tidow, H.,Andreeva, A.,Rutherford, T.J.,Fersht, A.R. Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold. J. Mol. Biol., 371:948-958, 2007 Cited by PubMed Abstract: 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. PubMed: 17594908DOI: 10.1016/j.jmb.2007.05.024 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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