Extended Data Fig. 4: Structural features of LHCGR.
From: Structures of full-length glycoprotein hormone receptor signalling complexes
a, Ribbon presentation of CGα and CGβ subunits stabilized by cysteine-knots. Disulfide bonds are shown as yellow sticks. b, Ribbon presentation of CGα and CGβ subunits. The C terminus of the CGβ subunit, known as ‘seat belt’ highlighted in red, circulates the CGα subunit. c, A ‘hand-clasp’ binding fashion of CG to LHCGR from different views. CGα and CGβ subunits are shown in a surface presentation, and LHCGR is displayed as a ribbon. d, Structural comparison of free human CG (PDB code: 1HCN, green–yellow) with receptor-bound CG (light sea green), the conformational changes in four segments are highlighted in red rectangle. e, Structural comparison of seat belt between CG–LHCGR and FSH–FSHR (PDB code: 1XWD). The residue P107 in CGβ and P101 in FSHβ are shown as sticks. f, Conformational comparison of TM6 of inactive LHCGR with inactive rhodopsin (PDB code:1L9H, left panel) and inactive β2AR (PDB code: 5JQH, right panel). g, Electrostatic potential surface of CG. The positively charged pockets that interact with the hinge loop are highlighted in red circles. h, Concentration–response curves for point mutants at S277. Data from three independent experiments are presented as the mean ± s.e.m. i, The putative interaction between S277 in the hinge helix and N351 in the P10 region based on the model of the Org43553–CG–LHCGR–Gs complex.
