Fig. 5: DP1-Gs protein binding interface. | Nature Communications

Fig. 5: DP1-Gs protein binding interface.

From: Structural insights into the mechanism of activation and inhibition of the prostaglandin D2 receptor 1

Fig. 5

a, b Structural comparison of DP1-Gs complex (light colors) with β2AR-Gs (3SN6, dark colors), viewed within the lipid membrane (a) and from the intracellular side (b). In the intracellular view (b), most of Gs protein is hidden, with only α5 and αN helices of Gαs helices shown to demonstrate an ~15° clockwise rotation of Gs in DP1 compared to β2AR. c, d A more narrow intracellular cavity and a different orientation of the α5 helix in DP1 (c) compared to β2AR (d). e, f Details of the DP1-Gs protein interface shown in two different orientations. Salt bridges and hydrogen bonds are shown as red dashed lines. The following colors are used in this figure: receptor (salmon), Gαs (cyan), Gβ (brown), Gγ (violet), Nb-35 (green).

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