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Abstract

IN SILICO HOMOLOGY STRUCTURE, B-CELL AND T-CELL EPITOPES PREDICTION OF SERINE/THREONINE PROTEIN KINASE A AGAINST TUBERCULOSIS

*Jagbir Singh1, Sunil Verma2

1Krishna Devi Maheshwari Pharmacy College Bagar, Jhunjhunu, Rajasthan, India
2Maharishi Markandeshwar University, Mullana, Ambala, India.

ABSTRACT

In spite of effective prophylaxis by use of different drugs there has been increase in the resistance in the pathogen and an alternative is required due to resistance of drugs being prescribed. Like Cellular signaling protein kinases in eukaryotes the Mycobacterium tuberculosis and other bacterias kinases have large family which has been identified. The phosphorylation of Serine/Threonine protein kinaseA (PknA) enzyme plays an important role in cellular signaling transduction and this also gets autophosphorylated. And this phosphorylated enzyme is responsible for activation of different other enzymes participating in cell division, cell differentiation and cell growth. The inhibition of this enzyme will lead to the death of mtb which causes tuberculosis. Homology model of PknA was developed by SWISSMODEL online server has the correct stereochemistry as gauged from the Ramachandran plot and good 3-D structure compatibility as assessed by PROCHECK. Structure prediction of the membrane bound drug targets is done along with B-cell epitope and T-cell mapping that highlights the immunogenic part of a protein. Antigenic T-cell epitopes were identified one of which one (VTTTGNPPA) found to be undigested by cyanogens bromide, trypsinR, clostripain, proline Endopept, AspN can also act as B-cell epitope.

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