Macromolecular Docking Simulation to Identify Binding Site of FGB1 for Antifungal Compounds

Bulletin of the Korean chemical society

Keun Woo Lee¹  Sugunadevi Sakkiah¹  Prabhakaran Soundararajan¹  Byoung Ryong Jeong¹  Iyyakkannu Sivanesan¹ 

关键词: NaD1;    FGB1;    Homology modeling;    Molecular docking;    Antifungal compounds;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

Fusarium oxysporum, an important pathogen that mainly causes vascular or fusarium wilt disease which leads to economic loss. Disruption of gene encoding a heterotrimeric G-protein-β-subunit (FGB1), led to decreased intracellular cAMP levels, reduced pathogenicity, colony morphology, and germination. The plant defense protein, Nicotiana alata defensin (NaD1) displays potent antifungal activity against a variety of agronomically important filamentous fungi. In this paper, we performed a molecular modeling and docking studies to find vital amino acids which can interact with various antifungal compounds using Discovery Studio v2.5 and GRAMMX, respectively. The docking results from FGB1-NaD1 and FGB1-antifungal complexes, revealed the vital amino acids such as His64, Trp65, Ser194, Leu195, Gln237, Phe238, Val324 and Asn326, and suggested that the anidulafungin is a the good antifungal compound.The predicted interaction can greatly assist in understanding structural insights for studying the pathogen and host-component interactions.

【 授权许可】

Unknown