2uwq

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17594908 17594908]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17594908 17594908]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Andreeva, A.]]
[[Category: Andreeva, A.]]
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[[Category: Fersht, A.R.]]
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[[Category: Fersht, A R.]]
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[[Category: Rutherford, T.J.]]
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[[Category: Rutherford, T J.]]
[[Category: Tidow, H.]]
[[Category: Tidow, H.]]
[[Category: ank repeat]]
[[Category: ank repeat]]
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[[Category: ubiquitin-like]]
[[Category: ubiquitin-like]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:36:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:51:03 2008''

Revision as of 16:51, 21 February 2008


2uwq

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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

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