Keywords: Protein, Tetratrico Peptide Repeat Protein, Unclassified Drug, Homozygosity, Nonsense Mutation, Priority Journal, Protein Domain, Protein Engineering, Protein Function, Protein Protein Interaction, Protein Secondary Structure, Protein Structure, Review, Amino Acid Sequence, Animals, Humans, Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Binding, Protein Folding, Tertiary, Repetitive Sequences, Saccharomyces Cerevisiae Proteins,
Affiliations: *** IBB - CNR ***
Inst. of Biostructure and Bioimaging, CNR, Via Mezzocannone 6, 80134 Naples, Italy
Dept. Molec. Biophys. and Biochem., Department of Chemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, United States
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TPR proteins: the versatile helix
Tetratrico peptide repeat (TPR) proteins have several interesting properties, including their folding characteristics, modular architecture and range of binding specificities. In the past five years, many 3D structures of TPR domains have been solved, revealing at a molecular level the versatility of this basic fold. Here, we discuss the structure of TPRs and highlight the diversity of arrangements and functions that are associated with these ubiquitous domains. Genomic analyses of the distribution of TPR domains are presented along with implications for protein engineering.
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