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HERO ID
7464538
Reference Type
Journal Article
Subtype
Review
Title
Versatile TPR domains accommodate different modes of target protein recognition and function
Author(s)
Allan, RK; Ratajczak, T
Year
2011
Is Peer Reviewed?
Yes
Journal
Cell Stress and Chaperones
ISSN:
1355-8145
EISSN:
1466-1268
Volume
16
Issue
4
Page Numbers
353-367
Language
English
PMID
21153002
DOI
10.1007/s12192-010-0248-0
Web of Science Id
WOS:000291883900001
Abstract
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.
Keywords
Tetratricopeptide repeat domains; Hsp70/Hsp90 chaperone machinery; Steroid receptors; p67(phox); PEX5
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