1jqq

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(New page: 200px<br /><applet load="1jqq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqq, resolution 2.65&Aring;" /> '''Crystal structure of...)
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[[Image:1jqq.jpg|left|200px]]<br /><applet load="1jqq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jqq, resolution 2.65&Aring;" />
caption="1jqq, resolution 2.65&Aring;" />
'''Crystal structure of Pex13p(301-386) SH3 domain'''<br />
'''Crystal structure of Pex13p(301-386) SH3 domain'''<br />
==Overview==
==Overview==
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While the function of most small signaling domains is confined to binary, ligand interactions, the peroxisomal Pex13p SH3 domain has the unique, capacity of binding to two different ligands, Pex5p and Pex14p. We have, used this domain as a model to decipher its structurally independent, ligand binding sites. By the combined use of X-ray crystallography, NMR, spectroscopy, and circular dichroism, we show that the two ligands bind in, unrelated conformations to patches located at opposite surfaces of this, SH3 domain. Mutations in the Pex13p SH3 domain that abolish interactions, within the Pex13p-Pex5p interface specifically impair PTS1-dependent, protein import into yeast peroxisomes.
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While the function of most small signaling domains is confined to binary ligand interactions, the peroxisomal Pex13p SH3 domain has the unique capacity of binding to two different ligands, Pex5p and Pex14p. We have used this domain as a model to decipher its structurally independent ligand binding sites. By the combined use of X-ray crystallography, NMR spectroscopy, and circular dichroism, we show that the two ligands bind in unrelated conformations to patches located at opposite surfaces of this SH3 domain. Mutations in the Pex13p SH3 domain that abolish interactions within the Pex13p-Pex5p interface specifically impair PTS1-dependent protein import into yeast peroxisomes.
==About this Structure==
==About this Structure==
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1JQQ 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=1JQQ OCA].
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1JQQ 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=1JQQ OCA].
==Reference==
==Reference==
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[[Category: compact beta-barrel of five anti-parrallel beta-strands]]
[[Category: compact beta-barrel of five anti-parrallel beta-strands]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:29:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:40 2008''

Revision as of 11:25, 21 February 2008


1jqq, resolution 2.65Å

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Crystal structure of Pex13p(301-386) SH3 domain

Overview

While the function of most small signaling domains is confined to binary ligand interactions, the peroxisomal Pex13p SH3 domain has the unique capacity of binding to two different ligands, Pex5p and Pex14p. We have used this domain as a model to decipher its structurally independent ligand binding sites. By the combined use of X-ray crystallography, NMR spectroscopy, and circular dichroism, we show that the two ligands bind in unrelated conformations to patches located at opposite surfaces of this SH3 domain. Mutations in the Pex13p SH3 domain that abolish interactions within the Pex13p-Pex5p interface specifically impair PTS1-dependent protein import into yeast peroxisomes.

About this Structure

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

Reference

Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain., Douangamath A, Filipp FV, Klein AT, Barnett P, Zou P, Voorn-Brouwer T, Vega MC, Mayans OM, Sattler M, Distel B, Wilmanns M, Mol Cell. 2002 Nov;10(5):1007-17. PMID:12453410

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