STRUCTURAL STUDIES OF ASPARTIC ENDOPEPTIDASE pep2 FROM NEOSARTORYA FISHERICA USING HOMOLGY MODELING TECHNIQUES

Aspartic endo peptidase pep2 protein of neosartorya fisherica belongs from aspartic acid proteases that depend on aspartic acid residues for their catalytic activity. Catalytic mechanism has been proposed for the hydrolysis of proteins to peptides or free amino acids. It is accomplished the putative proteolytic activity of the conidial surface. Therefore, if it is not act like an allergen itself but on the conidial surface may well play an important role in the processing or signaling to allergens and causing different rare human infections such as (lung’s aspergillosis and mycotic keratitis). To understand its different aspects, 3D structure model of (AEP pep2) was generated according to the structural coordinates of template (Proteinase A) with the help of MODELLER (9v8) software. To validate the energy and geometry in the model used PROCHECK and web server ProSA which determines that the predicted model to be stable and flexible.