Extended Data Fig. 4: Representative density maps for apo- and sucralose-bound TAS1R2-TAS1R3 structures.
From: Structural and functional characterization of human sweet taste receptor
a, Cryo-EM density maps of representative regions in VFTD and CRD of apo TAS1R2-TAS1R3 heterodimer structure. b, Glycosylation sites in VFTD and CRD of the apo TAS1R2-TAS1R3 heterodimer, shown in ball sticks representation. Extra EM density around the side chains of these glycosylation sites is displayed. c, Cryo-EM density maps of representative regions in VFTD, CRD, TMD and ECL2 of sucralose-bound TAS1R2-TAS1R3 heterodimer structure. d, Cryo-EM density maps of loops in CRDs that insert into the VFTD dimerization interface in apo TAS1R2-TAS1R3 heterodimer structure. e, Cryo-EM density maps of extracellular regions of TMDs including the conserved disulfide bonds between ECL2 and TM3 in TAS1R2 and TAS1R3, respectively, in apo-state structure. f, Cryo-EM density maps for helices TM1-TM7 of transmembrane domain, ICL2 and ECL2 of TAS1R2 and TAS1R3, respectively, in apo-state structure. g, Structural comparison of TAS1R2 and TAS1R3 in apo state aligned with TMD.
