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 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.
Cortajarena
Aitziber L
AL
Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
Regan
Lynne
L
D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D004795:Enzyme Stability; D006360:Heat-Shock Proteins / Q000737:chemistry*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D010749:Phosphoprotein Phosphatases / Q000737:chemistry*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D008024:Ligands; D009687:Nuclear Proteins; D010455:Peptides; C489791:Stip1 protein, mouse; D010749:Phosphoprotein Phosphatases; C089641:protein phosphatase 5