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PROSITE documentation PDOC50005 [for PROSITE entry PS50005] |
The tetratrico peptide repeat (TPRs) [1] is a degenerate 34-amino acid repeated motif that is widespread among all organisms. In the cell, TPR containing proteins are localized in a variety of subcellular compartment, including the nucleus, the cytoplasm and mitochondria [2]. Processes involving TPR proteins include cell-cycle control, transcription repression, stress response, protein kinase inhibition, mitochondrial and peroxisomal protein transport and neurogenesis. TPR repeats mediate protein-protein interactions and the assembly of multiprotein complexes. The smallest functional unit that is widely used appears to be three tandem-TPR motifs [3].
Many 3D structures of TPR domains have been solved (see for example <PDB:1A17>) [4]. A single TPR contains two antiparallel α helices which pack into an open structure [4] 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. An additional capping helix at the C-terminus is present in almost all TPR structures solved to date. This helix could be essential for the solubility or stability of these isolated domains. The consensus sequence of a TPR is defined by a pattern of small and large hydrophobic amino acids. Turn-positions, both between the two helices of a single TPR and between the two adjacent TPRs, show conservation of helix-breaking residues [5].
Some of the proteins containing TPR repeats are listed below:
Two profiles were developed for this module, the first one picks up TPR repeat units while the second profile is 'circular' and will thus detects a region containing adjacent TPR repeats.
Last update:January 2004 / First entry.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Sikorski R.S. Boguski M.S. Goebl M. Hieter P. |
Title | A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. | |
Source | Cell 60:307-317(1990). | |
PubMed ID | 2404612 |
2 | Authors | Goebl M. Yanagida M. |
Title | The TPR snap helix: a novel protein repeat motif from mitosis to transcription. | |
Source | Trends Biochem. Sci. 16:173-177(1991). | |
PubMed ID | 1882418 |
3 | Authors | Lamb J.R. Tugendreich S. Hieter P. |
Title | Tetratrico peptide repeat interactions: to TPR or not to TPR? | |
Source | Trends Biochem. Sci. 20:257-259(1995). | |
PubMed ID | 7667876 |
4 | Authors | Das A.K. Cohen P.W. Barford D. |
Title | The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. | |
Source | EMBO J. 17:1192-1199(1998). | |
PubMed ID | 9482716 | |
DOI | 10.1093/emboj/17.5.1192 |
5 | Authors | D'Andrea L.D. Regan L. |
Source | Trends Biochem. Sci. 28:655-662(2003). |