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• W2607079881 abstract "Dectin-1 is a recently discovered pattern-recognition receptor that plays an important role in antifungal innate immunity, which acts a specific receptor for β-glucan (BG). The present study, aimed at clarifying effect of BG and a new analog, maltotriose (MT) on Dectin-1 receptor. We implemented molecular docking of MT on Dectin-1 along with model-independent all-atom-molecular dynamics simulations. Simulations were carried out at three levels of complexity: (1) Apo-Dectin-1; (2) BG:Dectin-1; (3) MT:Dectin-1. All three system complexes were undergone stability check before showing a comparative analysis. A characteristic feature, noted for the MT:Dectin-1, is a shifting of loops (loop1 and loop2) orientation towards atoms of MT, a broad interaction suggested a robust and tight binding on comparison with BG:Dectin-1. Free energy estimation corroborated the observation, which furthermore, made a close agreement by revealing contribution of energy components of interacting residues. In addition, cluster analysis of complexes exhibit a smooth continuous transition to a new confirmation, represented by a series of clusters each having a longer lifetime. Principal component analysis revealed a broken pipe at binding site of BG:Dectin-1 during movement of atoms whereas in MT:Dectin-1 exhibited wide band and high amplitude motion of atoms in trajectory, was due to loop orientation toward MT. Observation was further shown by measuring distances and hydrogen binding calculation. Simulations of the BG:Dectin-1 and MT:Dectin-1 complex revealed first time the influence of BG and MT ligands. This study might extend the knowledge of the BG and MT interaction on Dectin-1 and proposed further potential bioassay of MT." @default.
• W2607079881 created "2017-04-28" @default.
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• W2607079881 date "2017-06-01" @default.
• W2607079881 modified "2023-10-16" @default.
• W2607079881 title "The effect of β-glucan and its potential analog on the structure of Dectin-1 receptor" @default.
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• W2607079881 doi "https://doi.org/10.1016/j.jmgm.2017.04.014" @default.
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