Molecular docking in Nεcarboxymethyl lysine targeting scavenger receptor CD36
10.3969/j.issn.1009-0126.2019.05.018
- VernacularTitle:Nε羧甲基赖氨酸靶向清道夫受体CD36的分子对接研究
- Author:
Zhongqun WANG
1
;
Zhengyang BAO
;
Zhen SUN
;
Jinchuan YAN
;
Chen SHAO
;
Lihua LI
Author Information
1. 江苏省原子医学研究所
- Keywords:
receptors,scavenger;
antigens,CD36;
foam cells;
diabetes mellitus
- From:
Chinese Journal of Geriatric Heart Brain and Vessel Diseases
2019;21(5):519-521
- CountryChina
- Language:Chinese
-
Abstract:
Objective To study whether Nεcarboxymethyl lysine(CML)can form a good molecular docking with the scavenger receptor CD36and induce a stable interaction.Methods The interaction between CML and CD36was studied by co-immunoprecipitation.The binding mode and affinity of CD36to CML were tested using AutoDock 4.2,iBabel and XQuartz-2.7.7software respectively. Results Co-immunoprecipitation showed that anti-CD36antibody magnetic bead could precipitate CD36from the total protein in RAW264.7cells and anti-CML could detect CD36 binding CML.CD36had a good molecular docking with CML,CD36and CML interacted stably with each other.The affinity of CML to 4Q4Bprotein structure of CD4extracellular domain was -29.62kJ/mol.ARG82,ASN71and THR70were the products of amino acid receptor interaction. Further docking analysis showed that CML could form 3interacting hydrogen bonds with 4Q4B,and the docking prediction inhibition constant was 6.92with a root mean square deviation of 2.54.Conclusion A good molecular docking between CML and 4Q4Bprotein structure of CD36extracellular domain can induce a stable interaction between CML and CD36.Hydrogen bonding is the main interaction mode.
