Cited by 260Protein Structure and DynamicsReceptor Mechanisms and SignalingHemoglobin structure and function

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Controlling Allosteric Networks in Proteins

Dokholyan, Nikolay V.·2016·Chemical Reviews

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Abstract

Allosteric transition, defined as conformational changes induced by ligand binding, is one of the fundamental properties of proteins. Allostery has been observed and characterized in many proteins, and has been recently utilized to control protein function via regulation of protein activity. Here, we review the physical and evolutionary origin of protein allostery, as well as its importance to protein regulation, drug discovery, and biological processes in living systems. We describe recently developed approaches to identify allosteric pathways, connected sets of pairwise interactions that are responsible for propagation of conformational change from the ligand-binding site to a distal functional site. We then present experimental and computational protein engineering approaches for control of protein function by modulation of allosteric sites. As an example of application of these approaches, we describe a synergistic computational and experimental approach to rescue the cystic-fibrosis-associated protein cystic fibrosis transmembrane conductance regulator, which upon deletion of a single residue misfolds and causes disease. This example demonstrates the power of allosteric manipulation in proteins to both elucidate mechanisms of molecular function and to develop therapeutic strategies that rescue those functions. Allosteric control of proteins provides a tool to shine a light on the complex cascades of cellular processes and facilitate unprecedented interrogation of biological systems.

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Authors: Dokholyan, N. V.
Affiliations: University of North Carolina at Chapel Hill (US)
Corresponding author: Dokholyan, Nikolay V.
ORCID: Dokholyan, Nikolay V.
Venue: Chemical Reviews
Publisher: American Chemical Society (ACS)
Published: 2016-02-19
Volume: 116
Issue: 11
Pages: 6463-6487
ISSN: 0009-2665 (ISSN-L)
1520-6890
DOI: 10.1021/acs.chemrev.5b00544
OpenAlex: W2283716387
Cited by: 260
References: 333
Citations by year: 2026: 11 · 2025: 21 · 2024: 24 · 2023: 48 · 2022: 23 · 2021: 31 · 2020: 27 · 2019: 28 · 2018: 21 · 2017: 18 · 2016: 7
FWCI: 2.23
Type: journal article
Language: en
Open access: closed
Locations: Chemical Reviews (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Allergy and Infectious Diseases (R01 AI102732)
National Institute of General Medical Sciences (5 R01 GM080742)
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 › Biochemistry › Hemoglobin structure and function
Keywords: protein allostery, allosteric networks, allosteric pathways, ligand-induced conformational change, protein regulation, protein engineering, cystic fibrosis transmembrane conductance regulator, CFTR, protein misfolding, drug discovery
MeSH terms: Allosteric Regulation, Allosteric Site, Humans, Ligands, Proteins, Cystic Fibrosis Transmembrane Conductance Regulator, Protein Structure, Quaternary, Focal Adhesion Protein-Tyrosine Kinases, Molecular Dynamics Simulation

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Controlling Allosteric Networks in Proteins

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