title: Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module.
abstract: Tetra-trico-peptide repeat (TPR) domains are found in numerous proteins, where they serve as interaction modules and multiprotein complex mediators. TPRs can be found in all kingdoms of life and regulate diverse biological processes, such as organelle targeting and protein import, vesicle fusion, and biomineralization. This review considers the structural features of TPR domains that permit the great ligand-binding diversity of this motif, given that TPR-interacting partners display variations in both sequence and secondary structure. In addition, tools for predicting TPR-interacting partners are discussed, as are the abilities of TPR domains to serve as protein-protein interaction scaffolds in biotechnology and therapeutics.
authors.affiliation: Department of Life Sciences, Ben-Gurion University of the Negev and National Institute for Biotechnology in the Negev, P.O. Box 653, Beer Sheva 84105, Israel.
authors.forename: Natalie
authors.initials: N
authors.lastname: Zeytuni
authors.forename: Raz
authors.initials: R
authors.lastname: Zarivach
mesh_terms: D000595:Amino Acid Sequence; D019281:Dimerization; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: D008024:Ligands; D046912:Multiprotein Complexes; D010455:Peptides