International Journal of Biotechnology & Biochemistry

Proteases and their specific inhibitors are ubiquitously distributed in the animal, plant and micro organism kingdoms, and play key regulatory roles in many biological processes, including the blood coagulation system, the complement cascade, apoptosis and the hormone processing pathways. In present work we have performed structural analysis of the interactions of proteases with their inhibitors in known structures of the proteases-inhibitors complexes. Trypsin and thrombin, the two best studied proteases are the focal point of the study. We have formulated a mechanistic structural perspective about the properties that define the specificity of the binding interface between these inhibitors and serine proteases. We have interpreted the nature of interaction of serine proteases with their inhibitors at atomic level and also analyzed energy perspectives of these interactions. Finally, we compared and found our modeled proteases of pathogenic organisms have almost no homology with the proteases of human genome.