LilrB2 is a kind of protein targeted by Aβ (1-42) oligomers. The binding of them may result in some symptoms related to Alzheimer’s disease. It’s important to explore the binding mechanisms for the design of inhibitors. Three different conformations were designed by molecular docking of lilrB2 and double-stranded Aβ (16-21), and were used as the initial conformations for molecular dynamics simulations. Three sets of data were analyzed, finding that the ASP23 residue on lilrB2 had a strong interaction with LYS residue on the chain of Aβ (16-21), which had an obvious effect on the binding of receptor and ligand. In different binding states, the interaction of CYS142 residue with VAL or PHE on the chain of Aβ (16-21) and the interaction of SER24 residue with ALA on the chain of Aβ (16-21) are favorable for the binding of receptor and ligand.
WU Wenze
,
LI Xiaoyi
. Binding of lilrB2 and double-stranded Aβ(16-21)[J]. Journal of University of Chinese Academy of Sciences, 2022
, 39(6)
: 727
-731
.
DOI: 10.7523/j.ucas.2020.0031
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