1nm7

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(New page: 200px<br /><applet load="1nm7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nm7" /> '''Solution structure of the ScPex13p SH3 domai...)
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[[Image:1nm7.gif|left|200px]]<br /><applet load="1nm7" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nm7.gif|left|200px]]<br /><applet load="1nm7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nm7" />
caption="1nm7" />
'''Solution structure of the ScPex13p SH3 domain'''<br />
'''Solution structure of the ScPex13p SH3 domain'''<br />
==Overview==
==Overview==
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Pex13p is an essential component of the peroxisomal protein import, machinery and interacts via its C-terminal SH3 domain with the type II, SH3-ligand Pex14p and the non-PXXP protein Pex5p. We report the solution, structure of the SH3 domain of Pex13p from Saccharomyces cerevisiae and, the identification of a novel-binding pocket, which binds a, non-PXXP-peptide representing the binding site of Pex5p. Chemical shift, assays revealed the binding sites for Pex5p and Pex14p ligand peptides to, be distinct and spatially separated. Competition assays demonstrated that, the two ligand peptides can bind simultaneously to the SH3 domain.
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Pex13p is an essential component of the peroxisomal protein import machinery and interacts via its C-terminal SH3 domain with the type II SH3-ligand Pex14p and the non-PXXP protein Pex5p. We report the solution structure of the SH3 domain of Pex13p from Saccharomyces cerevisiae and the identification of a novel-binding pocket, which binds a non-PXXP-peptide representing the binding site of Pex5p. Chemical shift assays revealed the binding sites for Pex5p and Pex14p ligand peptides to be distinct and spatially separated. Competition assays demonstrated that the two ligand peptides can bind simultaneously to the SH3 domain.
==About this Structure==
==About this Structure==
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1NM7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NM7 OCA].
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1NM7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM7 OCA].
==Reference==
==Reference==
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[[Category: Hong, X.]]
[[Category: Hong, X.]]
[[Category: Oschkinat, H.]]
[[Category: Oschkinat, H.]]
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[[Category: Pires, J.R.]]
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[[Category: Pires, J R.]]
[[Category: Schneider-Mergener, J.]]
[[Category: Schneider-Mergener, J.]]
[[Category: Volkmer-Engert, R.]]
[[Category: Volkmer-Engert, R.]]
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[[Category: yeast]]
[[Category: yeast]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:23:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:36 2008''

Revision as of 12:07, 21 February 2008


1nm7

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Solution structure of the ScPex13p SH3 domain

Overview

Pex13p is an essential component of the peroxisomal protein import machinery and interacts via its C-terminal SH3 domain with the type II SH3-ligand Pex14p and the non-PXXP protein Pex5p. We report the solution structure of the SH3 domain of Pex13p from Saccharomyces cerevisiae and the identification of a novel-binding pocket, which binds a non-PXXP-peptide representing the binding site of Pex5p. Chemical shift assays revealed the binding sites for Pex5p and Pex14p ligand peptides to be distinct and spatially separated. Competition assays demonstrated that the two ligand peptides can bind simultaneously to the SH3 domain.

About this Structure

1NM7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The ScPex13p SH3 domain exposes two distinct binding sites for Pex5p and Pex14p., Pires JR, Hong X, Brockmann C, Volkmer-Engert R, Schneider-Mergener J, Oschkinat H, Erdmann R, J Mol Biol. 2003 Mar 7;326(5):1427-35. PMID:12595255

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