The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
- PMID: 10517866
- DOI: 10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N
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 alpha-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.
Copyright 1999 John Wiley & Sons, Inc.
Similar articles
-
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.FEBS J. 2005 Jan;272(1):166-79. doi: 10.1111/j.1432-1033.2004.04397.x. FEBS J. 2005. PMID: 15634341
-
Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif.J Mol Biol. 2004 Oct 22;343(3):731-45. doi: 10.1016/j.jmb.2004.08.026. J Mol Biol. 2004. PMID: 15465058
-
An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei.J Mol Biol. 2001 Mar 16;307(1):271-82. doi: 10.1006/jmbi.2000.4465. J Mol Biol. 2001. PMID: 11243819
-
Pharmacological interference with protein-protein interactions mediated by coiled-coil motifs.Handb Exp Pharmacol. 2008;(186):461-82. doi: 10.1007/978-3-540-72843-6_19. Handb Exp Pharmacol. 2008. PMID: 18491064 Review.
-
Sel1-like repeat proteins in signal transduction.Cell Signal. 2007 Jan;19(1):20-31. doi: 10.1016/j.cellsig.2006.05.034. Epub 2006 Jul 25. Cell Signal. 2007. PMID: 16870393 Review.
Cited by
-
A little sugar goes a long way: the cell biology of O-GlcNAc.J Cell Biol. 2015 Mar 30;208(7):869-80. doi: 10.1083/jcb.201501101. J Cell Biol. 2015. PMID: 25825515 Free PMC article. Review.
-
The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.EMBO J. 2012 Mar 21;31(6):1506-17. doi: 10.1038/emboj.2011.472. Epub 2012 Jan 6. EMBO J. 2012. PMID: 22227520 Free PMC article.
-
The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly.Biophys Rev. 2023 Sep 12;15(6):1951-1965. doi: 10.1007/s12551-023-01127-9. eCollection 2023 Dec. Biophys Rev. 2023. PMID: 38192347 Free PMC article. Review.
-
Highly dynamic exon shuffling in candidate pathogen receptors ... what if brown algae were capable of adaptive immunity?Mol Biol Evol. 2012 Apr;29(4):1263-76. doi: 10.1093/molbev/msr296. Epub 2011 Dec 5. Mol Biol Evol. 2012. PMID: 22144640 Free PMC article.
-
Structure of minimal tetratricopeptide repeat domain protein Tah1 reveals mechanism of its interaction with Pih1 and Hsp90.J Biol Chem. 2012 Feb 17;287(8):5698-709. doi: 10.1074/jbc.M111.287458. Epub 2011 Dec 16. J Biol Chem. 2012. PMID: 22179618 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases