상세 보기
초록
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-beta-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 anti fungal 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.
키워드
- 제목
- Macromolecular Docking Simulation to Identify Binding Site of FGB1 for Antifungal Compounds
- 저자
- Soundararajan, Prabhakaran; Sakkiah, Sugunadevi; Sivanesan, Iyyakkannu; Lee, Keun Woo; Jeong, Byoung Ryong
- 발행일
- 2011-10-20
- 유형
- Article
- 권
- 32
- 호
- 10
- 페이지
- 3675 ~ 3681