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]
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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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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