Most of the available software to understand the relationship between the three-dimensional (3D) structure of a protein with its function, is based on the protein primary structure (i.e., protein sequence). That is, provided a group of homologue protein sequences, it is possible to identify critical residues for a protein function, assuming that those will be conserved along the group of homologue proteins. The assumption that conserved residues are indeed critical for a protein function has been systematically evaluated and showed that this is not always the case (1, 2).

It is clear that protein function arises from the interaction among the protein's residues. Such interactions are observed when the protein folds in a three dimensional shape. This fact may explain that primary sequence alone can not identify every critical residues correctly. At the same time, highligths the need to develop approaches aimed to identify critical residues from protein 3D structures.

Although several approaches based on physics principles (e.g., electrostatics) have been reported to identify critical residues from the three dimensional structure of proteins (3), there is a limited accessibility to software aimed to identify critical residues from protein structures. Network analysis on the other hand has been recently shown to be succesfull and complementary to protein sequence-based approaches (1, 4, 5).

This web site was designed to give access to software developed in our group aimed to identify critical residues from protein 3D structures. Three types of interfaces are included in this site: a web server and single or multi-computer applications. All these interfaces are developed in Java.

For any enquiries related to the use of this software, please contact us at gdelrio@ifc.unam.mx.

We appreciate your interest in our work.