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

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 antipa...

Full description

Saved in:
Bibliographic Details
Published inBioEssays Vol. 21; no. 11; pp. 932 - 939
Main Authors Blatch, Gregory L., Lässle, Michael
Format Journal Article
LanguageEnglish
Published New York John Wiley & Sons, Inc 01.11.1999
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary: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.
Bibliography:Wellcome Trust Biomedical Research Collaboration Grant - No. 053027
ArticleID:BIES5
istex:AD735386C5E428860D38BE9D33B0DA2530EEC0AD
University of the Witwatersrand Research Council Grant
ark:/67375/WNG-V5P7GG8F-1
The South African Foundation for Research and Development
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Feature-3
ObjectType-Review-1
ISSN:0265-9247
1521-1878
DOI:10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N