1n5z
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n5z OCA], [http://www.ebi.ac.uk/pdbsum/1n5z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n5z RCSB]</span> | ||
}} | }} | ||
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[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:49 2008'' |
Revision as of 19:25, 30 March 2008
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| , resolution 2.70Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Complex structure of Pex13p SH3 domain with a peptide of Pex14p
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
1N5Z is a Protein complex structure of sequences 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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