Identification of hot-spot residues in protein-protein interactions by computational docking

Background: The study of protein-protein interactions is becoming increasingly important for biotechnological and therapeutic reasons. We can define two major areas therein: the structural prediction of protein-protein binding mode, and the identification of the relevant residues for the interaction (so called 'hot-spots'). These hot-spot residues have high interest since they are considered one of the possible ways of disrupting a protein-protein interaction. Unfortunately, large-scale experimental measurement of residue contribution to the binding energy, based on alanine-scanning experiments, is costly and thus data is fairly limited. Recent computational approaches for hot-spot prediction have been reported, but they usually require the structure of the complex. Results: We have applied here normalized interface propensity (NIP) values derived from rigidbody docking with electrostatics and desolvation scoring for the prediction of interaction hotspots. This parameter ide...

• Type: Journal
• Year: 2008
• Where: BMCBI
• Authors: Solène Grosdidier, Juan Fernández-Recio
• Keywords: BMCBI 2008, Hot-spot Residues, Protein-protein Binding Mode, Protein-protein Interactions