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首页> 外文期刊>Journal of Biomolecular Structure and Dynamics >Homology modeling, molecular dynamics, and docking studies of pattern-recognition transmembrane protein-lipopolysaccharide and beta-1,3 glucan-binding protein from Fenneropenaeus indicus
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Homology modeling, molecular dynamics, and docking studies of pattern-recognition transmembrane protein-lipopolysaccharide and beta-1,3 glucan-binding protein from Fenneropenaeus indicus

机译：费氏线虫的模式识别跨膜蛋白-脂多糖和β-1,3葡聚糖结合蛋白的同源性建模，分子动力学和对接研究

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摘要

Lipopolysaccharide and beta-1,3 glucan-binding protein (LGBP) is a family of pattern-recognition transmembrane proteins (PRPs) which plays a vital role in the immune mechanism of crustaceans in adverse conditions. Fenneropenaeus indicus LGBP-deduced amino acid has conserved potential recognition motif for beta-1,3 linkages of polysaccharides and putative RGD (Arg-Gly-Asp) cell adhesion sites for the activation of innate defense mechanism. In order to understand the stimulating activity of beta-1,3 glucan (beta-glucan) and its interaction with LGBP, a 3D model of LGBP is generated. Molecular docking is performed with this model, and the results indicate Arg71 with strong hydrogen bond from RGD domain of LGBP. Moreover, from the docking studies, we also suggest that Arg34, Lys68, Val135, and Ala146 in LGBP are important amino acid residues in binding as they have strong bonding interaction in the active site of LGBP. In our in vitro studies, yeast agglutination results suggest that shrimp F. indicus LGBP possesses sugar binding and recognition sites in its structure, which is responsible for agglutination reaction. Our results were synchronized with the already reported evidence both in vivo and in vitro experiments. This investigation may be valuable for further experimental investigation in the synthesis of novel immunomodulator.
机译：脂多糖和β-1,3葡聚糖结合蛋白（LGBP）是模式识别跨膜蛋白（PRP）的家族，在不良条件下甲壳动物的免疫机制中起着至关重要的作用。 Fenneropenaeus indicus LGBP推导的氨基酸保留了多糖β-1,3键和潜在RGD（Arg-Gly-Asp）细胞粘附位点的潜在识别基序，以激活先天防御机制。为了了解β-1,3葡聚糖（β-葡聚糖）的刺激活性及其与LGBP的相互作用，生成了LGBP的3D模型。用该模型进行分子对接，结果表明Arg71具有来自LGBP RGD结构域的强氢键。此外，从对接研究中，我们还建议LGBP中的Arg34，Lys68，Val135和Ala146是重要的结合氨基酸残基，因为它们在LGBP的活性位点具有很强的键合相互作用。在我们的体外研究中，酵母凝集的结果表明，虾印度对虾LGBP在其结构中具有糖结合和识别位点，这是造成凝集反应的原因。我们的结果与体内和体外实验中已报道的证据同步。该研究对于合成新型免疫调节剂的进一步实验研究可能是有价值的。

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