Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0185928
Title: Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold
Authors: Ivanov S.M.
Cawley A.
Huber R.G.
Bond P.J. 
Warwicker J.
Keywords: protein protein interaction
static electricity
alpha helix
amino acid sequence
bacterium
binding site
chemical phenomena
chemistry
conserved sequence
human
kinetics
metabolism
protein domain
sequence alignment
sequence homology
thermodynamics
amino acid
bacterial protein
bacterial toxin
DNA binding protein
DNA topoisomerase IV
membrane protein
parD protein, Bacteria
protein binding
ubiquitin conjugating enzyme
ubiquitin protein ligase
VapB protein, Bacteria
Amino Acid Sequence
Amino Acids
Bacteria
Bacterial Proteins
Bacterial Toxins
Binding Sites
Conserved Sequence
DNA Topoisomerase IV
DNA-Binding Proteins
Humans
Hydrophobic and Hydrophilic Interactions
Kinetics
Membrane Glycoproteins
Protein Binding
Protein Conformation, alpha-Helical
Protein Interaction Domains and Motifs
Sequence Alignment
Sequence Homology, Amino Acid
Static Electricity
Thermodynamics
Ubiquitin-Conjugating Enzymes
Ubiquitin-Protein Ligases
Issue Date: 2017
Citation: Ivanov S.M., Cawley A., Huber R.G., Bond P.J., Warwicker J. (2017). Protein-protein interactions in paralogues: Electrostatics modulates specificity on a conserved steric scaffold. PLoS ONE 12 (10) : e0185928. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0185928
Rights: Attribution 4.0 International
Abstract: An improved knowledge of protein-protein interactions is essential for better understanding of metabolic and signaling networks, and cellular function. Progress tends to be based on structure determination and predictions using known structures, along with computational methods based on evolutionary information or detailed atomistic descriptions. We hypothesized that for the case of interactions across a common interface, between proteins from a pair of paralogue families or within a family of paralogues, a relatively simple interface description could distinguish between binding and non-binding pairs. Using binding data for several systems, and large-scale comparative modeling based on known template complex structures, it is found that charge-charge interactions (for groups bearing net charge) are generally a better discriminant than buried non-polar surface. This is particularly the case for paralogue families that are less divergent, with more reliable comparative modeling. We suggest that electrostatic interactions are major determinants of specificity in such systems, an observation that could be used to predict binding partners. © 2017 Ivanov et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/161171
ISSN: 19326203
DOI: 10.1371/journal.pone.0185928
Rights: Attribution 4.0 International
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This item is licensed under a Creative Commons License Creative Commons