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Protein Science (2006), 15:1193-1198. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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FOR THE RECORD

Ligand binding by TPR domains

Aitziber L. Cortajarena1 and Lynne Regan1,2

1 Department of Molecular Biophysics & Biochemistry
2 Department of Chemistry, Yale University, New Haven, Connecticut 06520, USA

(RECEIVED January 10, 2006; FINAL REVISION January 10, 2006; ACCEPTED February 9, 2006)

Tetratricopeptide repeat (TPR) domains bind specific peptide ligands and are thought to mediate protein–protein interactions in a variety of biological systems. Here we compare peptide ligand-binding by several different TPR domains. We present specific examples that demonstrate that TPR domains typically undergo little or no structural rearrangement upon ligand binding. Our data suggest that, contrary to a recent proposal, coupled folding and binding is not the common mechanism of ligand recognition by TPR domains.

Keywords: tetratricopeptide repeat (TPR); Hsp90; protein phosphatase 5 (PP5); Vpu-binding protein/small glutamine-rich protein (UBP/SGT); ligand binding


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