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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:
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| The amino-terminal TPR domain of human Hop bound to a carboxy-terminal peptide from Hsp70 (red). | |
