CAPRI (Comparative Analysis of PRotein-protein Interaction)

Studies involving protein structures most often deal with a large amount of information. To understand the process of protein-protein interactions is necessary to study the process that occurs in this molecular interface. Interactions can be observed at the residue level, but it is known that they occur in reality at the atomic level. Several paradigms propose different ways to define atomic interactions, and it is known that it is necessary to compare these paradigms to improve our understanding of the molecular interactions allowing to expand our knowledge of the many mechanisms and cellular functions.

Thus, we propose here the CAPRI database for comparative analysis of three different paradigms that are used to define contacts in protein-protein interface. CAPRI has information of about 45,000 protein complexes containing data about interactions between pairs of atoms, residue and chains. Four types of interactions are investigated: hydrogen bonds, hydrophobic interactions, ionic and aromatic stacking.