Author(s): Gromiha MM, Yokota K, Fukui K
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Abstract The binding sites in protein-protein complexes have been identified with different methods including atomic contacts, reduction in solvent accessibility and interaction energy between the interacting partners. In our earlier work, we have developed an energy-based criteria for identifying the binding sites in protein-protein complexes, which showed that the interacting residues are different from that obtained with distance-based methods. In this work, we analyzed the binding site residues based on sequence and structural properties, such as, neighboring residues, secondary structure, solvent accessibility, conservation of residues, medium and long-range contacts and surrounding hydrophobicity. Our results showed that the neighboring residues of binding sites in proteins and ligands are different from each other although the interacting pairs of residues have a common behavior. The analysis on surrounding hydrophobicity reveals that the binding residues are less hydrophobic than non-binding sites, which suggests that the hydrophobic core are important for folding and stability whereas the surface seeking residues play a critical role in binding. This tendency has been verified with the number of contacts in binding sites. In addition, the binding site residues are highly conserved compared with non-binding residues. We suggest that the incorporation of sequence and structure-based features may improve the prediction accuracy of binding sites in protein-protein complexes. 2009 Elsevier B.V. All rights reserved.
This article was published in Int J Biol Macromol
and referenced in Journal of Bioequivalence & Bioavailability