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
-
Building Better Barrels - β-barrel Biogenesis and Insertion in Bacteria and Mitochondria.J Mol Biol. 2021 Aug 6;433(16):166894. doi: 10.1016/j.jmb.2021.166894. Epub 2021 Feb 24. J Mol Biol. 2021. PMID: 33639212 Free PMC article. Review.
-
Conserved Ser/Arg-rich motif in PPZ orthologs from fungi is important for its role in cation tolerance.J Biol Chem. 2012 Mar 2;287(10):7301-12. doi: 10.1074/jbc.M111.299438. Epub 2012 Jan 9. J Biol Chem. 2012. PMID: 22232558 Free PMC article.
-
Identification and phylogenetic analysis of RNA binding domain abundant in apicomplexans or RAP proteins.Microb Genom. 2021 Mar;7(3):mgen000541. doi: 10.1099/mgen.0.000541. Epub 2021 Mar 3. Microb Genom. 2021. PMID: 33656416 Free PMC article.
-
Enterococcal Rgg-like regulator ElrR activates expression of the elrA operon.J Bacteriol. 2013 Jul;195(13):3073-83. doi: 10.1128/JB.00121-13. Epub 2013 May 3. J Bacteriol. 2013. PMID: 23645602 Free PMC article.
-
The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex.Nat Commun. 2024 Sep 8;15(1):7844. doi: 10.1038/s41467-024-52321-6. Nat Commun. 2024. PMID: 39245686 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases