![]() ![]() PBP-2′ has three striking regulatory points constituted by first penicillin binding site at Ser25, second penicillin binding site at Ser405, and finally a single metallic ligand binding site at Glu657 which binds to ions. Our analysis revealed that the PBP-2′ is very stable with more hydrophilic amino acids expressing antigenic sites. We conducted a complete structural and functional regulatory analysis of PBP-2′ protein. Presently, there is no structural and regulatory information on PBP-2′ protein. The PBP-2′ functions by substituting other penicillin binding proteins which have been inhibited by β-lactam antibiotics. A mechanism for resistance has been proposed in which methicillin resistant Staphylococcus aureus (MRSA) isolates acquired a new protein called β-lactam inducible penicillin binding protein (PBP-2′). Resistance to methicillin by Staphylococcus aureus is a persistent clinical problem worldwide. ![]()
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