Microtubules are tubulin polymers present in the eukaryotic cytoskeleton essential for structural stability and cell division that are also roadways for intracellular transport of vesicles and organelles. In the human malaria parasite\u00a0Plasmodium falciparum<\/i>, apart from providing structural stability and cell division, microtubules also facilitate important biological activities crucial for parasite survival in hosts, such as egression and motility. Hence, parasite structures and processes involving microtubules are among the most important drug targets for discovering much-needed novel\u00a0Plasmodium<\/i>\u00a0inhibitors. The current study aims to construct reliable and high-quality 3D models of \u03b1-, \u03b2-, and \u03b3-tubulins using various modeling techniques. We identified a common binding pocket specific to\u00a0Plasmodium<\/i>\u00a0\u03b1-, \u03b2-, and \u03b3-tubulins. Molecular dynamics simulations confirmed the stability of the\u00a0Plasmodium<\/i>\u00a0tubulin 3D structures. The models generated in the present study may be used for protein\u2013protein and protein\u2013drug interaction investigations targeted toward designing malaria parasite tubulin-specific inhibitors.<\/p>\n
Click here to know more:-\u00a0https:\/\/pubs.acs.org\/doi\/10.1021\/acsomega.1c01988<\/a><\/p>\n\n\n