Molecular docking of anthocyanins constituents and HER-2 kinase domain.
- Author:
Liping LUO
;
Xiaoping YU
;
Bin HAN
;
Xiangyan CHEN
;
Xiaoli PENG
;
Wei CHEN
;
Jie ZHOU
;
Suiyan LI
- Publication Type:Journal Article
- MeSH:
Anthocyanins;
chemistry;
Catalytic Domain;
Hydrogen Bonding;
Hydrophobic and Hydrophilic Interactions;
Molecular Docking Simulation;
Phosphorylation;
Protein Interaction Domains and Motifs;
Receptor, ErbB-2;
chemistry
- From:
Chinese Journal of Biotechnology
2014;30(3):504-513
- CountryChina
- Language:Chinese
-
Abstract:
Anthocyanins are a ubiquitous group of water-soluble plant pigments of the flavonoid family, with anticancer property through HER-2 signaling pathway. Nowadays, molecular docking plays an important role in exposing the active sites and obtaining the bioactive conformation involving protein-ligand interactions. According to the crystal structure of HER-2 kinase domain and 12 main antitumor compounds of anthocyanins as well as ATP, a molecular docking study was performed by MVD program. All 12 compounds could bind to the same cavity of HER-2 kinase domain by high affinity (MolDock Score < -105 kJ/mol for anthocyanidins, < -130 kJ/mol for anthocyanidins-glc), where hydrophobic force and hydrogen bond played key roles. Additionally, this cavity overlapped with ATP binding (MolDock Score = -161 kJ/mol) domain; the binding of anthocyanins presumably interfered the H bond formation between ATP and HER-2. These results indicate that anthocyanins may competitively bind to ATP binding site in HER-2 kinase domain by suppressing HER-2 activation and downstream signaling cascade. This may provide useful theoretical instruction for the molecular mechanism of HER-2 kinase activity inhibition by anthocyanins in cancer prevention and treatment.
