Molecular mechanisms of protein-protein recognition: Whether the surface placed charged residues determine the recognition process?

We studied the structure and composition of contact areas in 812 different kind dimeric protein-protein complexes from Brookhaven data base (PDB) in o rder to reveal their pecularities with regard to protein-protein recognitio n. We have found, that the large portion of complexes (similar to 70%) have oppositely charged residues in the contact areas (interfaces) on the subun its surfaces, which form electrostatic contacts - R:E, RD, K:E, K:D, H:E, H :D. These results are consistent with the current view that high rate compl ex formation may be driven by the long-range electrostatic interaction betw een charged AA residues of subunits surfaces.