He Zhang
1 Key Laboratory of the glucolipid metabolism, college of life science and technology, Dalian university, Dalian 116000, Liaoning, ChinaJingda Li
1 Key Laboratory of the glucolipid metabolism, college of life science and technology, Dalian university, Dalian 116000, Liaoning, ChinaAmei Chen
2 Department of Histology and Embryology, Inner Mongolia medical university, Hohhot 010000, Inner Mongolia, ChinaQingping Liu
1 Key Laboratory of the glucolipid metabolism, college of life science and technology, Dalian university, Dalian 116000, Liaoning, ChinaNational Natural Science Foundation of China (No. 81270361).
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.
张鹤,李敬达,陈阿梅,刘庆平. 血浆糖蛋白β2-GPI分子结构域与ox-LDL结合机制[J]. Chinese Journal of Biotechnology, 2017, 33(1): 122-131
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