Binding of glycoprotein β₂-GPI with oxidized low density lipoprotein / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 122-131, 2017.
Article
in Chinese
| WPRIM
| ID: wpr-310555
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Type of study:
Prognostic study
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2017
Type:
Article
Similar
MEDLINE
...
LILACS
LIS