Structural highlights
Function
[PEX13_YEAST] Component of the peroxisomal translocation machinery with PEX14 and PEX17. Interacts with the PTS1 receptor (PAS10/PEX5). [PEX14_YEAST] Component of the peroxisomal translocation machinery with PEX13 and PEX17. Interacts with both the PTS1 and PTS2 receptors. Binds directly to PEX17.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Douangamath A, Filipp FV, Klein AT, Barnett P, Zou P, Voorn-Brouwer T, Vega MC, Mayans OM, Sattler M, Distel B, Wilmanns M. Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain. Mol Cell. 2002 Nov;10(5):1007-17. PMID:12453410
