Structural analysis of protein translocase subunit SecY from Mycobacterium tuberculosis H37Rv: a potential target for anti-tuberculosis drug discovery Online publication date: Fri, 24-Nov-2017
by Tilahun Melak Sitote; Sunita Gakkhar
International Journal of Computational Biology and Drug Design (IJCBDD), Vol. 10, No. 4, 2017
Abstract: Identification of noble drug targets is a very important step in the development of anti-mycobacterial drugs to counter the problem of drug resistance. The availability of structural information of a specified drug target is one of the druggablity criteria. However, many proteins do not have experimentally solved structure in spite of the efforts of structural genomics projects. In this study, structural analysis on a selected potential drug target of Mycobacterium tuberculosis H37Rv has been carried out. Protein translocase subunit SecY (Rv0732) has been selected since it is a highly ranked potential drug target without solved three-dimensional structure. In silico structural analysis has been carried out to get descriptive three-dimensional structure. The models were generated using crystal structure of Secye Translocon from Thermus thermophilus with a fab fragment (2ZJS_Y) as a template. The active site has been identified for protein-inhibitor binding.
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