2uwq: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwq OCA], [http://www.ebi.ac.uk/pdbsum/2uwq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uwq RCSB]</span> | |||
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[[Category: ubiquitin-like]] | [[Category: ubiquitin-like]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:05:34 2008'' | ||
Revision as of 05:05, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF ASPP2 N-TERMINUS
OverviewOverview
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.
About this StructureAbout this Structure
2UWQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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