Abstract
The tetratricopeptide repeat (TPR) motif is one of many repeat motifs that form structural domains in proteins that can act as interaction scaffolds in the formation of multi-protein complexes involved in numerous cellular processes such as transcription, the cell cycle, protein translocation, protein degradation and host defence against invading pathogens. The crystal structures of many TPR domain-containing proteins have been determined, showing TPR motifs as two anti-parallel α-helices packed in tandem arrays to form a structure with an amphipathic groove which can bind a target peptide. This is however not the only mode of target recognition by TPR domains, with short amino acid insertions and alternative TPR motif conformations also shown to contribute to protein interactions, highlighting diversity in TPR domains and the versatility of this structure in mediating biological events.
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References
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Acknowledgements
Research in the authors’ laboratory is supported by the National Health & Medical Research Council of Australia and the National Breast Cancer Foundation. The authors are also grateful to Carmel Cluning and Danny Mok for assistance in preparing the manuscript.
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Allan, R.K., Ratajczak, T. Versatile TPR domains accommodate different modes of target protein recognition and function. Cell Stress and Chaperones 16, 353–367 (2011). https://doi.org/10.1007/s12192-010-0248-0
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DOI: https://doi.org/10.1007/s12192-010-0248-0