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. Author manuscript; available in PMC: 2017 Nov 24.
Published in final edited form as: Nature. 2017 May 24;546(7657):248–253. doi: 10.1038/nature22394

Extended Data Figure 10. Comparison of G protein trimer structures from activated GLP-1R:Gs:Nb35 complex and T4L-β2AR:Gs:Nb35 complex with alignment on GαsRas alone, related to Figure 5.

Extended Data Figure 10

a, Views of superposition of G protein trimer structures from the activated GLP-1R:Gs structure (GαsRas in gold, Gβ in light blue, Gγ in dark blue) and T4L-β2AR:Gs structure (all colored in grey). b, Schematic representation of recognition between C-terminus of α5-helix (H387-L394) and active receptors of β2AR (c) and GLP-1R (d). The sequence of C-terminus of α5-helix (H387-L394) is shown in the middle in gold. Residues involving in the interaction with α5-helix (H387-L394) in the receptor of β2AR (green box) and GLP-1R (orchid box) are shown over and below, respectively. Hydrophobic interactions are shown in blue and polar interactions in red. Ballesteros-Weinstein numbering in superscript is shown.