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Fig. 4 Docking result of GA2P. The protein structure of S1P1 (PDB code
3V2Y) is shown in the ribbon model and the residues surrounding the
binding site are shown in the line model. GA2P and ML5 (the bound ligand
in 3V2Y) are represented in the stick model. The carbon atoms are high-
lighted in yellow (GA2P) and cyan (ML5). The oxygen, nitrogen, and
phosphate atoms are shown in red, blue, and orange, respectively. GA2P
binds to the binding pocket with a binding affinity of À8.1 kcal molÀ1. The
aliphatic C-15 tail fills the hydrophobic pocket, and the head group
interacts with the S1P1 residues Lys34, Tyr39, Asn101, and Arg120 within
hydrogen-bonding distance.
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extract library. There were structural similarities between this
naturally-occurring SMS inhibitor and sphingolipid, which
suggests that the inhibitor was a mimic of the original mole-
cule. Modified ceramide mimic derivatives were prepared to
selectively inhibit SMS2, which is valuable in understanding
SMS biology. Analysis of the S1P ginkgolic acid 2-phosphate
mimic activity on the S1P receptor supported this ‘‘sphingo-
mimic’’ concept. Several natural products that have a hydro-
philic core and hydrophobic hydrocarbon side chain have been
characterized, such as cardols, urushiols, and gentisides.20
Our study implied that the physiological activities of these
compounds work through lipid-related systems.
`
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´
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The authors acknowledge the Innovation COE project for
Future Medicine and Medicinal Research.
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Conflicts of interest
There are no conflicts to declare.
Notes and references
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This journal is ©The Royal Society of Chemistry 2018
Chem. Commun., 2018, 54, 12758--12761 | 12761