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A computational tool to predict the evolutionarily conserved protein–protein interaction hot‐spot residues from the structure of the unbound protein
Author(s) -
Agrawal Neeraj J.,
Helk Bernhard,
Trout Bernhardt L.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.11.004
Subject(s) - hot spot (computer programming) , protein–protein interaction , protein function , protein structure , function (biology) , computational biology , chemistry , biology , biophysics , biochemistry , genetics , computer science , gene , operating system
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.