The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

Abstract

The tetratricopeptide repeat (TPR) motif is a protein‐protein interaction module found in multiple copies in a number of functionally different proteins that facilitates specific interactions with a partner protein(s). Three‐dimensional structural data have shown that a TPR motif contains two antiparallel α‐helices such that tandem arrays of TPR motifs generate a right‐handed helical structure with an amphipathic channel that might accommodate the complementary region of a target protein. Most TPR‐containing proteins are associated with multiprotein complexes, and there is extensive evidence indicating that TPR motifs are important to the functioning of chaperone, cell‐cycle, transcription, and protein transport complexes. The TPR motif may represent an ancient protein‐protein interaction module that has been recruited by different proteins and adapted for specific functions. BioEssays 1999;21:932–939. © 1999 John Wiley & Sons, Inc.

RNA editing in plant organelles: machinery, physiological function and evolution

“…The PPR motif is structurally similar to the TPR (tetratricopeptide repeat) motif consisting of 34 amino acids [36,38]. The tandem arrays of TPR motifs are expected to function in protein-protein interactions [39]. However, genetic evidence suggests that PPR motifs may bind to 700 T. Shikanai RNA editing in plant organelles specific RNA sequences (table 1), as do some TPR motifs [40,41].…”

Bardet-Biedl syndrome: an emerging pathomechanism of intracellular transport

“…BBS1, BBS2 and BBS7 proteins have predicted β-propeller domains, which are relatively common motifs with multiple functions [36]. BBS4 and BBS8 harbour several tetratricopeptide repeat domains (TPRs), which are found in many different proteins and play important roles in protein-protein interactions [37]. BBS5 possesses two DM16 repeat motifs of unknown function, and BBS9 was previously annotated as human B1 protein whose function is not known.…”

A novel role for DYX1C1, a chaperone protein for both Hsp70 and Hsp90, in breast cancer

“…A TPR domain is deWned by a repeating motif of 34 amino acids that adopt a helix-turn-helix secondary structure (Blatch and Lassle 1999). The concave and convex surfaces at the inner and outer interfaces (D'Andrea and Regan 2003) of this domain facilitate the binding of various ligands.…”