Conserved residue clusters at protein-protein interfaces and their use in binding site identification

Background: Biological evolution conserves protein residues that are important for structure and function. Both protein stability and function often require a certain degree of structural co-operativity between spatially neighboring residues and it has previously been shown that conserved residues occur clustered together in protein tertiary structures, enzyme active sites and protein-DNA interfaces. Residues comprising protein interfaces are often more conserved compared to those occurring elsewhere on the protein surface. We investigate the extent to which conserved residues within protein-protein interfaces are clustered together in three-dimensions. Results: Out of 121 and 392 interfaces in homodimers and heterocomplexes, 96.7 and 86.7%, respectively, have the conserved positions clustered within the overall interface region. The significance of this clustering was established in comparison to what is seen for the subsets of the same size of randomly selected residues from the int...

• Type: Journal
• Year: 2010
• Where: BMCBI
• Authors: Mainak Guharoy, Pinak Chakrabarti
• Keywords: BMCBI 2010, Conserved Residues, Protein, Protein Residues