TY - JOUR AU - Bhatt, Tarun K. PY - 2012/11/05 Y2 - 2024/03/29 TI - Structural Characterization of Histone Deacetylase from Plasmodium Falciparum JF - Asian Journal of Science and Applied Technology JA - AJSAT VL - 1 IS - 2 SE - Articles DO - 10.51983/ajsat-2012.1.2.733 UR - https://ojs.trp.org.in/index.php/ajsat/article/view/733 SP - 28-30 AB - <p>Histone deacetylase (HDAC) is the key enzyme responsible for epigenetic regulation of an organism. This protein has been involved in transcriptional regulation of many proteins associated with chromatin remodelling. Homologs of histone deacetylase are also found in malaria parasite Plasmodium falciparum where it plays major role in regulation of key pathways of parasite. In this study, we determined the three-dimensional structure of histone deacetylase from Plasmodium falciparum (PfHDAC) by using homology modelling tools available at Swiss Modeller server and Modweb. Modelled structure was alidated using Ramachandran plot and active site determination was performed using CASTp. We believe that structural analysis of PfHDAC could be pivotal in discovering new drug like molecules against malaria parasite.</p> ER -