Mapping allosteric communications within individual proteins
| Autor: | Abha Jain, Craig Gambogi, Nikolay V. Dokholyan, Andrew L. Lee, Leanna R. McDonald, Jian Wang |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Cellular activity Cell signaling Computer science Science Allosteric regulation General Physics and Astronomy Methyl-Accepting Chemotaxis Proteins Computational biology Molecular Dynamics Simulation 010402 general chemistry 01 natural sciences General Biochemistry Genetics and Molecular Biology Article Protein Structure Secondary 03 medical and health sciences Computational biophysics Protein structure Allosteric Regulation Computational platforms and environments Protein Interaction Mapping Escherichia coli Animals Humans Ohm Enzyme Inhibitors lcsh:Science Protein function Network architecture Internet Multidisciplinary Network topology Escherichia coli Proteins Proteins General Chemistry Jian wang 0104 chemical sciences 030104 developmental biology lcsh:Q Algorithms Allosteric Site Software |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Allostery in proteins influences various biological processes such as regulation of gene transcription and activities of enzymes and cell signaling. Computational approaches for analysis of allosteric coupling provide inexpensive opportunities to predict mutations and to design small-molecule agents to control protein function and cellular activity. We develop a computationally efficient network-based method, Ohm, to identify and characterize allosteric communication networks within proteins. Unlike previously developed simulation-based approaches, Ohm relies solely on the structure of the protein of interest. We use Ohm to map allosteric networks in a dataset composed of 20 proteins experimentally identified to be allosterically regulated. Further, the Ohm allostery prediction for the protein CheY correlates well with NMR CHESCA studies. Our webserver, Ohm.dokhlab.org, automatically determines allosteric network architecture and identifies critical coupled residues within this network. The computational prediction of protein allostery can guide experimental studies of protein function and cellular activity. Here, the authors develop a network-based method to detect allosteric coupling within proteins solely based on their structures, and set up a webserver for allostery prediction. |
| Databáze: | OpenAIRE |
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