Article
Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain.
Molecular cell - 1 Nov 2002
Douangamath Alice, Filipp Fabian V, Klein André T J, Barnett Phil, Zou Peijian, Voorn-Brouwer Tineke, Vega M Cristina, Mayans Olga M, Sattler Michael, Distel Ben, Wilmanns Matthias
Abstract excerpt
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...
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