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Allostery without a conformational change? Revisiting the paradigm

Nussinov, Ruth, Tsai, Chung-Jung·2015·Current Opinion in Structural Biology

DOI 10.1016/j.sbi.2014.11.005

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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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Self-citation
An allosteric site enables fine‐tuning of cathepsin K by diverse effectors
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Authors: Nussinov, R., & Tsai, C.-J.
Affiliations: Tel Aviv University (IL)
Frederick National Laboratory for Cancer Research (US)
Corresponding author: Nussinov, Ruth
ORCID: Nussinov, Ruth
Tsai, Chung-Jung
Venue: Current Opinion in Structural Biology
Publisher: Elsevier BV
Published: 2015-02
Volume: 30
Pages: 17-24
ISSN: 0959-440X (ISSN-L)
DOI: 10.1016/j.sbi.2014.11.005
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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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Allostery without a conformational change? Revisiting the paradigm

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