The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Versatile TPR domains accommodate different modes of target protein recognition and function
Open accessAbstract
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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Structure of TPR Domain–Peptide Complexes
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A New First Step in Activation of Steroid Receptors
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The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
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Self-citationStructure of the TPR Domain of p67phox in Complex with Rac·GTP
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Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation
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Cited by
Jackson, S. E. (2012) · Topics in Current Chemistry · doi:10.1007/128_2012_356 · Cited by 338
Zhang, H., Amick, J., Chakravarti, R., Santarriaga, S., Schlanger, S., McGlone, C., Dare, M., Nix, J. C., Scaglione, K. M., Stuehr, D. J., et al. (2015) · Structure · doi:10.1016/j.str.2015.01.003 · Cited by 98
Mouse models of human ocular disease for translational research
Krebs, M. P., Collin, G. B., Hicks, W. L., Yu, M., Charette, J. R., Shi, L. Y., Wang, J., Naggert, J. K., Peachey, N. S., & Nishina, P. M. (2017) · PLOS ONE · doi:10.1371/journal.pone.0183837 · Cited by 51
Chaperoning the Mononegavirales: Current Knowledge and Future Directions
Latorre, V., Mattenberger, F., & Geller, R. (2018) · Viruses · doi:10.3390/v10120699 · Cited by 14
Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates
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Metadata
- Authors
- Allan, R. K., & Ratajczak, T.
- Venue
- Cell Stress and Chaperones
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 16
- Issue
- 4
- Pages
- 353-367
- ISSN
- 1355-8145 (ISSN-L)
- OpenAlex
- W2069871720
- Cited by
- 247
- References
- 27
- FWCI
- 4.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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