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Tetratricopeptide repeat
PDB 1a17 EBI.jpg
Symbol TPR_1
Pfam PF00515
Pfam clan CL0020
InterPro IPR001440
SCOP 1a17
CDD cd00189

The tetratricopeptide repeat (TPR) is a structural motif. It consists in a degenerate 34 amino acid sequence motif identified in a wide variety of proteins. It is found in tandem arrays of 3–16 motifs,[1] which form scaffolds to mediate protein–protein interactions and often the assembly of multiprotein complexes. These repeats usually fold together to produce a single, linear solenoid domain called TPR domain. Proteins with such domains include the anaphase-promoting complex (APC) subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the PKR protein kinase inhibitor, the major receptor for peroxisomal matrix protein import PEX5 and mitochondrial import proteins.


The structure of the PP5 protein was the first structure to be determined. The structure solved by X-ray crystallography by Das and colleagues showed that the TPR sequence motif was composed of a pair of antiparallel alpha helices.[2] The PP5 structure contained 3 tandem TPR repeats which showed the sequential TPR repeats formed an alpha-helical solenoid structure.


Human genes encoding proteins containing this motif include:


  1. ^ Blatch GL, Lässle M (November 1999). "The tetratricopeptide repeat: a structural motif mediating protein-protein interactions". BioEssays 21 (11): 932–9. doi:10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N. PMID 10517866. 
  2. ^ Das AK, Cohen PW, Barford D (March 1998). "The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions". EMBO J. 17 (5): 1192–9. doi:10.1093/emboj/17.5.1192. PMC 1170467. PMID 9482716. 

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