The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Structural and Energetic Basis of Allostery
Open accessAbstract
Allostery is a biological phenomenon of fundamental importance in regulation and signaling, and efforts to understand this process have led to the development of numerous models. In spite of individual successes in understanding the structural determinants of allostery in well-documented systems, much less success has been achieved in identifying a set of quantitative and transferable ground rules that provide an understanding of how allostery works. Are there organizing principles that allow us to relate structurally different proteins, or are the determinants of allostery unique to each system? Using an ensemble-based model, we show that allosteric phenomena can be formulated in terms of conformational free energies of the cooperative elements in a protein and the coupling interactions between them. Interestingly, the resulting allosteric ground rules provide a framework to reconcile observations that challenge purely structural models of site-to-site coupling, including (a) allostery in the absence of pathways of structural distortions, (b) allostery in the absence of any structural change, and (c) the ability of allosteric ligands to act as agonists under some circumstances and antagonists under others. The ensemble view of allostery that emerges provides insights into the energetic prerequisites of site-to-site coupling and thus into how allostery works.
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Cites
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Cited by
The ensemble nature of allostery
Motlagh, H. N., Wrabl, J. O., Li, J., & Hilser, V. J. (2014) · Nature · doi:10.1038/nature13001 · Cited by 1,247
Self-citationWei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Allostery in Its Many Disguises: From Theory to Applications
Wodak, S. J., Paci, E., Dokholyan, N. V., Berezovsky, I. N., Horovitz, A., Li, J., Hilser, V. J., Bahar, I., Karanicolas, J., Stock, G., et al. (2019) · Structure · doi:10.1016/j.str.2019.01.003 · Cited by 404
Self-citationA Unified View of “How Allostery Works”
Tsai, C.-J., & Nussinov, R. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003394 · Cited by 401
Controlling Allosteric Networks in Proteins
Dokholyan, N. V. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00544 · Cited by 260
Metadata
- Authors
- Hilser, V. J., Wrabl, J. O., & Motlagh, H. N.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2012-06-09
- Volume
- 41
- Issue
- 1
- Pages
- 585-609
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2112907786
- Cited by
- 317
- References
- 63
- FWCI
- 1.56
- Type
- journal article
- Language
- en
- Open access
- green
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- Hilser, V. J., Wrabl, J. O., & Motlagh, H. N. (2012). Structural and Energetic Basis of Allostery. Annual Review of Biophysics. https://doi.org/10.1146/annurev-biophys-050511-102319
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