supplementary material for the article · 2017-03-07 · supplementary material . for the article:...
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SUPPLEMENTARY MATERIAL
For the article:
Molecular requirements involving the human platelet protease-
activated receptor-4 mechanism of activation by peptide
analogues of its tethered-ligand
By Moschonas et al.
Figure S1. A. Sequence alignment between PAR-1 and PAR-4 as predicted using Prime (in
red are shown the conserved residues); B. Ramachandran plot for the resulting homology
model (favorable region is shown in green, allowed region in blue and disallowed region in
red);
Figure S2. Predicted cavities as possible binding sites in PAR-4 revealed using SiteID.
Figure S3: Three-dimensional and two-dimensional docking pose of the Ac-AYPGKF-NH2
peptide in the PAR-4 structure.
Figure S4: Three-dimensional and two-dimensional docking pose of the trans-cinnamoyl-
AYPGKF-NH2 peptide in the PAR-4 structure.
Figure S5: Three-dimensional and two-dimensional docking pose of the YPGKF-NH2
peptide in the PAR-4 structure.
Figure S6: Three-dimensional and two-dimensional docking pose of the Ac-YPGKF-NH2
peptide in the PAR-4 structure.
Figure S7: Three-dimensional and two-dimensional docking pose of the caffeoyl-YPGKF-
NH2 peptide in the PAR-4 structure.
Figure S8: Three-dimensional and two-dimensional docking pose of YD-3 in the PAR4
structure.
Figure S9: Three-dimensional and two-dimensional docking pose of ML-354 in the PAR-4
structure.
Figure S10: Three-dimensional and two-dimensional docking pose of BMS-986120 in the
PAR-4 structure.
Figure S11: Superposition of the docking poses of the three small molecules [A. YD-3; B.
ML-354; C. BMS-986120 (shown in purple)] that act as antagonists for PAR-4 and the
docking pose of trans-cinnamoyl-YPGKF-NH2 (shown in green). The most important
residues involved in the binding of both the peptide and the small molecules are shown in
gray color.