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Faryal Ashraf , Atia tul Wahab , Muhammad Iqbal Choudhary (Dr . Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Kar ac hi, Karachi 75270, Pakistan)
Staphylococcus aureus is both a normal flora, and also an opportunistic pathogen of human body It causes a range of diseases, from minor infections to threatening diseases Enzymes are amongst fundamental biomolecules that regulates cell cycle, developmental stages and cellular metabolism inside the living organisms Targeting enzyme subunits either regulatory or catalytic that bring profound effect on enzyme performance would result in regulation (inhibition or activation) of a particular reaction It would also render the subsequent pathway to be blocked or initiate This study explored the interaction analysis of one of the smallest and most conserved proteins in genus Staphylococcus i e purS subunit of phosphoribosyl formylglycinamidine synthase This complex enzyme catalyzes the fourth step reaction of denovo purine biosynthesis in bacteria PurS subunit thus play a critical role in DNA and RNA synthesis Therefore, purS is considered as a valid drug target During the current study, phosphoribosyl formylglycinamidine synthase PurS protein was cloned, expressed, and purified in high yield The purified protein was subjected to interaction analysis with FDA approved drugs using STD NMR