2uwq: Difference between revisions
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'''SOLUTION STRUCTURE OF ASPP2 N-TERMINUS''' | '''SOLUTION STRUCTURE OF ASPP2 N-TERMINUS''' | ||
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[[Category: Rutherford, T J.]] | [[Category: Rutherford, T J.]] | ||
[[Category: Tidow, H.]] | [[Category: Tidow, H.]] | ||
[[Category: | [[Category: Ank repeat]] | ||
[[Category: | [[Category: Apoptosis]] | ||
[[Category: | [[Category: Aspp2]] | ||
[[Category: | [[Category: Cell cycle]] | ||
[[Category: | [[Category: Sh3-binding]] | ||
[[Category: | [[Category: Sh3-domain]] | ||
[[Category: | [[Category: Ubiquitin-like]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:41:06 2008'' | |||
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Revision as of 14:41, 4 May 2008
SOLUTION STRUCTURE OF ASPP2 N-TERMINUS
Overview
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 Structure
2UWQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 17:41:06 2008
