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TPR Domain

No ImageTPR motifs exhibit a large degree of sequence diversity. However, structural comparison reveals a highly conserved three dimensional structure. Individual TPR domains are composed of two anti-parallel alpha helices separated by a turn. Multiple TPR domains arrange at regular angles and form a right-handed superhelix. This creates a groove with a large amount of surface area available for ligand binding.

Structure Reference:
Scheufler, C. et al. (2000) Cell. 101(2): 199-210. PDB: 1ELW.

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.
Examples of Proteins: 
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
p67phox GTP-Rac surface contacts

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