Computational analysis, structural modeling and ligand binding site prediction of Plasmodium falciparum 1-deoxy-d-xylulose-5-phosphate synthase

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• 作者：Achintya Mohan Goswami ^{achintya02@gmail.com}
• 关键词：Plasmodium falciparum ; Apicoplast ; 1-Deoxy-d-xylulose-5-phosphate synthase ; Homology modeling ; In silico ; Methyl erythritol phosphate pathway
• 刊名：Computational Biology and Chemistry
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：66
• 期：Complete
• 页码：1-10
• 全文大小：4736 K
• 卷排序：66

文摘

Plasmodium falciparum 1-deoxy-d-xylulose-5-phosphate synthase (DXP synthase) is predicted to be stable and residues forming pyrimidine binding pocket are evolutionary conserved. Comparative homology based modeling of DXP synthase is carried out using HHPred, Raptor X and (PS)2 web server and Modeller to get structural insights. Theoretical validation of model reveals that structure generated by Modeller provides better results. Presence of five cavities along with magnesium and thiamine diphosphate binding residues of DXP synthase are predicted in details. Virtual screening of ZINC database identifies ten potential compounds in thiamine diphosphate binding region of the enzyme.