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2uwq

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[[Image:2uwq.jpg|left|200px]]<br /><applet load="2uwq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2uwq.jpg|left|200px]]
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caption="2uwq" />
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'''SOLUTION STRUCTURE OF ASPP2 N-TERMINUS'''<br />
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{{Structure
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|PDB= 2uwq |SIZE=350|CAPTION= <scene name='initialview01'>2uwq</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''SOLUTION STRUCTURE OF ASPP2 N-TERMINUS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2UWQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWQ OCA].
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2UWQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWQ OCA].
==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://www.ncbi.nlm.nih.gov/pubmed/17594908 17594908]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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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 Thu Feb 21 18:51:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:40:38 2008''

Revision as of 16:40, 20 March 2008


PDB ID 2uwq

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Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 18:40:38 2008

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