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- W2891601160 abstract "We analyzed the binding of P.rβ₂-GPI-DV with ox-LDL by fluorescence, molecular simulation and circular dichroism. We used SDS-PAGE and Western blotting to identify the purity of P.rβ₂-GPI-DV, fluorescence, circular dichroism spectroscopy and molecular docking simulation to analyze the binding between P.rβ₂-GPI-DV and oxLDL. P.rβ₂-GPI-DV was specifically recognized by anti-His antibody at 12 kDa position. The chromophoric groups, the changes of secondary structure and the molecular docking simulations revealed that the active pocket formed by Cys281-Lys-Asn-Lys-Glu-Lys-Lys287 and Leu313-Ala-Phe-Trp316 of P.rβ₂-GPI-DV and the -COOH carboxyl of oxLig-1 were the key for binding. P.rβ₂-GPI combined with ox-LDL via the fifth functional domain and the -COOH group. Our findings provide theoretical basis to further study the binding between β₂-GPI and ox-LDL in serum.通过酵母重组P.rβ₂-GPI-DV (β₂ 糖蛋白I 第5 结构域) 蛋白的荧光、圆二色谱及分子对接模拟，分析血浆糖蛋白β₂-GPI-DV 分子结构域与ox-LDL 的结合机制。SDS-PAGE、Western blotting 验证重组蛋白P.rβ₂-GPI-DV 表达正确性及纯度；荧光、圆二色光谱、分子对接模拟解析重组蛋白与oxLDL、oxLDL 配体oxLig-1可能存在的结合机制和位点。SDS-PAGE、Western blotting 显示，在12 kDa 大小处有目的蛋白存在且与特异性抗体结合；荧光、圆二色谱的发色基团、二级结构的变化趋势及分子对接模拟结果揭示，P.rβ₂-GPI-DV 的Cys281-Lys-Asn-Lys-Glu-Lys-Lys287 和Leu313-Ala-Phe-Trp316 区域组成的活性口袋与oxLig-1 的ω-COOH 羧基是实现二者结合的关键。以上结果表明，β₂-GPI 通过其第5 结构域 (DV) 的赖氨酸阳性区域与ox-LDL 的ω-COOH 基团识别结合，为血清中β₂-GPI 特异性结合ox-LDL 的机制研究提供理论依据。." @default.
- W2891601160 created "2018-09-27" @default.
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- W2891601160 date "2017-01-25" @default.
- W2891601160 modified "2023-09-23" @default.
- W2891601160 title "[Binding of glycoprotein β₂-GPI with oxidized low density lipoprotein]." @default.
- W2891601160 doi "https://doi.org/10.13345/j.cjb.160178" @default.
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