Conservation and coevolution at the protein-protein interface increase with the number of interacting partners.

ELIN TEPPA; CRISTINA ESTER MARINO; CRISTINA MARINO-BUSLJE

CABA

Congreso; International Society for computational biology/Asoc. Arg de Bioinformática y Biol. Computacional; 2016

ISCB/A2B2C

BackgroundProtein-proteininteracting interfaces are under significant selection pressure to maintainspecific interactions throughout evolution. However, the evolutionary pressureis not homogeneous within aninterface, as each residue does not contribute equally to the binding energy of the complex. In order toconsider the functional differences of interface residues, the distinctionbetween rim and core areas of the interface has been proposed.   Residueconservation and coevolution are two evolutionary signals that can be extractedfrom a Multiple Sequence Alignment. These signals can be used to detect differential selection pressurebetween protein regions. Residue conservation and molecular coevolution aredirectly related with the functional importance of a residue. The principlebehind coevolution is that when a residue changes a compensatory mutationelsewhere in the protein takes place to preserve or restore the activity. The purpose of the study is to characterize theregions of protein interfaces defined by the core-rim model, by mean of twoevolutionary measures based on conservation and coevolution in a comprehensivedataset of 2947 protein complexes.