Ligand binding by TPR domains

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 typ...

Full description

Saved in:
Bibliographic Details
Published in:Protein science 2006-05, Vol.15 (5), p.1193-1198
Main Authors: Cortajarena, Aitziber L., Regan, Lynne
Format: Article
Language:English
Subjects:
Binding Sites
Carrier Proteins - chemistry
Circular Dichroism
Enzyme Stability
For the Record
Heat-Shock Proteins - chemistry
Hsp90
ligand binding
Ligands
Magnetic Resonance Spectroscopy
Models, Molecular
Nuclear Proteins - chemistry
Peptides - chemistry
Phosphoprotein Phosphatases - chemistry
Protein Folding
protein phosphatase 5 (PP5)
Protein Structure, Tertiary
Structure-Activity Relationship
tetratricopeptide repeat (TPR)
Thermodynamics
Vpu‐binding protein/small glutamine‐rich protein (UBP/SGT)
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.062092506