The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Allostery without a conformational change? Revisiting the paradigm
Abstract
Classically, allostery induces a functional switch through a conformational change. However, lately an increasing number of studies concluded that the allostery they observe takes place through sheer dynamics. Here we explain that even if a structural comparison between the active and inactive states does not detect a conformational change, it does not mean that there is no conformational change. We list likely reasons for this lack of observation, including crystallization conditions and crystal effects; one of the states is disordered; the structural comparisons disregard the quaternary protein structure; overlooking synergy effects among allosteric effectors and graded incremental switches and too short molecular dynamics simulations. Specific functions are performed by distinct conformations; they emerge through specific interactions between conformationally selected states.
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“AlphaFold, which predicts single ranked structures for a protein sequence, is unable to address directly allosteric mechanisms, which are based on the populations of conformational states in the ensembles.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [104]
Citations
Cites
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The role of dynamic conformational ensembles in biomolecular recognition
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Self-citationEvolutionarily Conserved Pathways of Energetic Connectivity in Protein Families
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Self-citationHaemoglobin: The structural changes related to ligand binding and its allosteric mechanism
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Self-citationAllostery in Disease and in Drug Discovery
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Research works printed but not linked: 1
- Blackmore, 2013, Three sites and you are out: ternary synergistic allostery controls aromatic amino acid biosynthesis in Mycobacterium tuberculosis, J Mol Biol, 425, 1582, 10.1016/j.jmb.2012.12.019 · DOI
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Catalysis and allostery in bacterial ATP phosphoribosyltransferases
Bates, L. G., & da Silva, R. G. (2026) · FEBS Journal · doi:10.1111/febs.70769
Metadata
- Authors
- Nussinov, R., & Tsai, C.-J.
- Affiliations
- Tel Aviv University (IL)
- Frederick National Laboratory for Cancer Research (US)
- Corresponding author
- Nussinov, Ruth
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2015-02
- Volume
- 30
- Pages
- 17-24
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2035586950
- Cited by
- 202
- References
- 65
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 9 · 2023: 18 · 2022: 14 · 2021: 19 · 2020: 13 · 2019: 26 · 2018: 15 · 2017: 27 · 2016: 37 · 2015: 7
- FWCI
- 2.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- allosteric regulation, conformational change, protein dynamics, allosteric effectors, quaternary structure, protein disorder, functional switch, protein conformational states
- MeSH terms
- Allosteric Regulation, Crystallization, Models, Biological, Models, Molecular, Protein Conformation, Molecular Dynamics Simulation
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