Tetratricopeptide

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

Structure[edit]

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.

Examples[edit]

Human genes encoding proteins containing this motif include:

References[edit]

  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. 

External links[edit]

Further reading[edit]