TPR Domain
The amino-terminal TPR domain of human Hop bound to a carboxy-terminal peptide from Hsp70 (red).
Domain Binding and Function
The tetratricopeptide repeat (TPR) motif was originally identified in yeast as a protein-protein interaction module in cell cycle proteins. It has since been found in organisms ranging from bacteria to humans. The TPR motif is a degenerate sequence of ~34 amino acids loosely based around the consensus residues -W-LG-Y-A-F-A-P-. The sequence occurs in tandem arrays and is present in over 800 different proteins. TPR motif-containing proteins act as scaffolds for the assembly of different multiprotein complexes including the anaphase promoting, the peroxisomal import receptor and the NADPH oxidase complexes.
Structure Reference
- Scheufler, C. et al. (2000) Cell 101(2), 199–210.
Examples of Domain Proteins
Binding Examples
| TPR Domain Proteins | Binding Partners | Peptide Ligands |
|---|---|---|
| PEX5 | PTS-1 target signal | S-K-L-COOH |
| Hop | Hsp70 - C-term heptapeptide Hsp90 - C-term pentapeptide |
E-E-V-D-COOH E-E-V-D-COOH |
| p67phox | GTP-Rac | surface contacts |
