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7464538 
Journal Article 
Review 
Versatile TPR domains accommodate different modes of target protein recognition and function 
Allan, RK; Ratajczak, T 
2011 
Yes 
Cell Stress and Chaperones
ISSN: 1355-8145
EISSN: 1466-1268 
16 
4 
353-367 
English 
21153002 
WOS:000291883900001 
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. 
Tetratricopeptide repeat domains; Hsp70/Hsp90 chaperone machinery; Steroid receptors; p67(phox); PEX5