The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor
Open accessAbstract
Intrinsically disordered proteins play critical but often poorly understood roles in mediating protein interactions. The interactions of disordered proteins studied to date typically entail structural stabilization, whether as a global disorder-to-order transition or minimal ordering of short linear motifs. The disordered cyclin-dependent kinase (CDK) inhibitor Sic1 interacts with a single site on its receptor Cdc4 only upon phosphorylation of its multiple dispersed CDK sites. The molecular basis for this multisite-dependent interaction with a single receptor site is not known. By NMR analysis, we show that multiple phosphorylated sites on Sic1 interact with Cdc4 in dynamic equilibrium with only local ordering around each site. Regardless of phosphorylation status, Sic1 exists in an intrinsically disordered state but is surprisingly compact with transient structure. The observation of this unusual binding mode between Sic1 and Cdc4 extends the understanding of protein interactions from predominantly static complexes to include dynamic ensembles of intrinsically disordered states.
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Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
The interplay between structure and function in intrinsically unstructured proteins
Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717
Systematic Discovery of New Recognition Peptides Mediating Protein Interaction Networks
Neduva, V., Linding, R., Su-Angrand, I., Stark, A., Masi, F. D., Gibson, T. J., Lewis, J., Serrano, L., & Russell, R. B. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030405 · Cited by 359
Variable Control of Ets-1 DNA Binding by Multiple Phosphates in an Unstructured Region
Pufall, M. A., Lee, G. M., Nelson, M. L., Kang, H.-S., Velyvis, A., Kay, L. E., McIntosh, L. P., & Graves, B. J. (2005) · Science · doi:10.1126/science.1111915 · Cited by 246
Self-citation
Cited by
Extreme disorder in an ultrahigh-affinity protein complex
Borgia, A., Borgia, M. B., Bugge, K., Kissling, V. M., Heidarsson, P. O., Fernandes, C. B., Sottini, A., Soranno, A., Buholzer, K. J., Nettels, D., et al. (2018) · Nature · doi:10.1038/nature25762 · Cited by 653
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Martin, E. W., & Holehouse, A. S. (2020) · Emerging Topics in Life Sciences · doi:10.1042/etls20190164 · Cited by 281
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Alderson, T. R., Pritišanac, I., Kolarić, Đ., Moses, A. M., & Forman-Kay, J. D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304302120 · Cited by 240
Self-citationFuzzy Complexes: A More Stochastic View of Protein Function
Fuxreiter, M., & Tompa, P. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0659-4_1 · Cited by 240
Metadata
- Authors
- Mittag, T., Orlicky, S., Choy, W.-Y., Tang, X., Lin, H., Sicheri, F., Kay, L. E., Tyers, M., & Forman-Kay, J. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-11-18
- Volume
- 105
- Issue
- 46
- Pages
- 17772-17777
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2107270569
- Cited by
- 343
- References
- 4
- FWCI
- 6.95
- Type
- journal article
- Language
- en
- Open access
- green
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- Mittag, T., Orlicky, S., Choy, W.-Y., Tang, X., Lin, H., Sicheri, F., Kay, L. E., Tyers, M., & Forman-Kay, J. D. (2008). Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0809222105
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