Fig. 3: Hydrophobic interactions between α5h and TMs 5 and 6.
From: Insights into G-protein coupling preference from cryo-EM structures of Gq-bound PTH1R
a, Overall comparison of the TM regions of Gq-bound and Gs-bound PTH1R. b, Comparison of the degree of opening in TMs 5 and 6 of the receptor and the angle of α5h of G protein in Gq-bound and Gs-bound PTH1R. c,d, Interactions between the PTH1R intracellular cavity and the G-protein α5h for Gq (c) and Gs (d). Notable residues are shown as stick and Corey–Pauling–Koltun (CPK) models. e,f, Contact frequencies between PTH1R and α5h measured in MD simulations. Residues with a contact frequency below 30% are omitted. Both heat maps represent the combined data from three independent replicate simulations. g,h. The SASA calculated in the MD simulations for Gq (g) and Gs (h). The total SASA was computed as the sum of I3815.57, L3855.61, L3895.65, S4096.41, V4126.44 and L4136.45 throughout three replicate simulations. Average values, calculated every 80 frames, are shown in bold.
