A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein

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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. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Agrawal, N. J., Helk, B., & Trout, B. L. (2014). A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein. FEBS Letters, 588(2), 326–333. https://doi.org/10.1016/j.febslet.2013.11.004

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