Cited by 102Protein Structure and DynamicsHeat shock proteins researchReceptor Mechanisms and Signaling

Coupling between global dynamics and signal transduction pathways: a mechanism of allostery for chaperonin GroEL

Chennubhotla, Chakra, Yang, Zheng, Bahar, Ivet·2008·Molecular BioSystems

Abstract

Despite significant efforts toward understanding the molecular basis of allosteric communication, the mechanisms by which local energetic and conformational changes cooperatively diffuse from ligand-binding sites to distal regions across the 3-dimensional structure of allosteric proteins remain to be established. Recent experimental and theoretical evidence supports the view that allosteric communication is facilitated by the intrinsic ability of the biomolecules to undergo collective changes in structure, triggered by ligand binding. Two groups of studies recently proved to provide insights into such intrinsic, structure-induced effects: elastic network models that permit us to visualize the cooperative changes in conformation that are most readily accessible near native state conditions, and information-theoretic approaches that elucidate the most efficient pathways of signal transmission favored by the overall architecture. Using a combination of these two approaches, we highlight, by way of application to the bacterial chaperonin complex GroEL-GroES, how the most cooperative modes of motion play a role in mediating the propagation of allosteric signals. A functional coupling between the global dynamics sampled under equilibrium conditions and the signal transduction pathways inherently favored by network topology appears to control allosteric effects.

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Crossref · 10.1039/b717819k

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  • Hiroshi Sugiyama's group has recently developed a new class of artificial TF mimics chemicals based on pyrrole-imidazole polyamides that can target specific DNA sequences and regulate gene expression.

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Authors
Chennubhotla, C., Yang, Z., & Bahar, I.
Affiliations
  • University of Pittsburgh (US)
  • Department of Computational Biology, School of Medicine, University of Pittsburgh a , Suite 3064 Biomedical Science Tower 3 3501 Fifth Ave., Pittsburgh, PA 15213, USA   bahar@ccbb.pitt.edu   +1 (412) 648-3163   +1 (412) 648-3332
Venue
Molecular BioSystems
Published
2008-02-20
Volume
4
Issue
4
Pages
287-292
ISSN
  • 1742-2051 (ISSN-L)
  • 1742-206X
OpenAlex
W1972964958
Cited by
102
References
50
Citations by year
2025: 2 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 1 · 2020: 9 · 2019: 7 · 2018: 1 · 2017: 9 · 2016: 4 · 2015: 3 · 2014: 8 · 2013: 10 · 2012: 7
FWCI
4.52
Type
journal article
Language
en
Open access
closed
Locations
  • Molecular BioSystems (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r33gm068400-03)
  • National Institute of General Medical Sciences (#R33 GM068400)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
allosteric communication, signaling pathways, elastic network model, information theory, cooperative conformational change, global dynamics, network topology, protein conformational dynamics
MeSH terms
Allosteric Regulation, Computer Simulation, Markov Chains, Models, Chemical, Models, Molecular, Protein Conformation, Signal Transduction, Chaperonin 60

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