SHP-1 molecular interaction. Insights from integrated sequence, evolutionary and structural data.

CALDEZ, MATÍAS JOSÉ; BARBERO, GASTÓN; GONZALEZ, HEIDI; FARGNOLI, LUCIA; TISCORNIA, MARÍA MERCEDES; ZAPATA, PEDRO DARÍO

Pekin

Congreso; 2012 6th International Conference on Bioinformatics and Biomedical Engeenering; 2012

IEEE - ICBBE

Protein-protein interactions are among the most difficult problem to achieve in the post genomic era. Many efforts were made to accomplish this problem using physicochemical approaches as well as structural analysis. The actual importance of deciphering the way that proteins interact is that they regulate many important cellular mechanisms like cell signaling, gene expression, and much other. In this work we aim to use a novel approach summarizing evolutionary, physicochemical and structural genomic data to elucidate the residues involved in the enzyme activity and surface interaction sites of proteins involved in the progression of the antiproliferative effect of somatostantine. We used PDB structures for all proteins involved and a docking technique was performed to obtain three complexes of SHP-1 protein with SSTR2, PI3K and nNOS. It is well known that protein interaction involve not only surface residues but also residues from the core of the protein as well as protein chain movements. In this context our approach can exploit determined structures to identify structurally conserved residues, which can be further used for binding site predictions as well as protein dynamics and movements.