A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein
Name
A Computational Tool to Predict the Evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein.pdf
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Author(s)
Agrawal, Neeraj J.
Helk, Bernhard
Trout, Bernhardt L.
Date Issued
November 2013
Journal
FEBS Letters
Publisher
Elsevier
Citation
Agrawal, Neeraj J., Bernhard Helk, and Bernhardt L. Trout. “A Computational Tool to Predict the Evolutionarily Conserved Protein-Protein Interaction Hot-Spot Residues from the Structure of the Unbound Protein.” FEBS Letters 588, no. 2 (November 12, 2013): 326–333.
Version
Author's final manuscript
Abstract
Identifying hot-spot residues – residues that are critical to protein–protein binding – can help to elucidate a protein's function and assist in designing therapeutic molecules to target those residues. We present a novel computational tool, termed spatial-interaction-map (SIM), to predict the hot-spot residues of an evolutionarily conserved protein–protein interaction from the structure of an unbound protein alone. SIM can predict the protein hot-spot residues with an accuracy of 36–57%. Thus, the SIM tool can be used to predict the yet unknown hot-spot residues for many proteins for which the structure of the protein–protein complexes are not available, thereby providing a clue to their functions and an opportunity to design therapeutic molecules to target these proteins.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
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Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/j.febslet.2013.11.004
