Versatile TPR domains accommodate different modes of target protein recognition and function

Cell Stress Chaperones. 2011 Jul;16(4):353-67. doi: 10.1007/s12192-010-0248-0. Epub 2010 Dec 9.


The tetratricopeptide repeat (TPR) motif is one of many repeat motifs that form structural domains in proteins that can act as interaction scaffolds in the formation of multi-protein complexes involved in numerous cellular processes such as transcription, the cell cycle, protein translocation, protein degradation and host defence against invading pathogens. The crystal structures of many TPR domain-containing proteins have been determined, showing TPR motifs as two anti-parallel α-helices packed in tandem arrays to form a structure with an amphipathic groove which can bind a target peptide. This is however not the only mode of target recognition by TPR domains, with short amino acid insertions and alternative TPR motif conformations also shown to contribute to protein interactions, highlighting diversity in TPR domains and the versatility of this structure in mediating biological events.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Crystallography, X-Ray
  • HSP70 Heat-Shock Proteins / chemistry*
  • HSP90 Heat-Shock Proteins / chemistry*
  • Humans
  • Molecular Chaperones / chemistry*
  • Phosphoproteins / chemistry
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Receptors, Steroid / chemistry
  • Repetitive Sequences, Amino Acid*


  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones
  • Phosphoproteins
  • Proteins
  • Receptors, Steroid
  • neutrophil cytosol factor 67K