Fig. 6: TSHR complex structural models and comparison of the TMH2 L471M variant.

a The entire complex model of herring TSHR with M471 highlighted in green (position 2.51) shows that this residue is outside the ligand or Gs-protein binding site. b Close-up view of M4712.51 reveals that the side chain is directed towards the membrane and surrounded by a tight hydrophobic patch. c Superimposition of herring and human TSHRs reveals similarities and differences within the hydrophobic patch and also the potential side-chain orientations of leucine (autumn herrTSHR), methionine (spring herrTSHR), and phenylalanine (humTSHR). The human TSHR side chains that differ from those of herring TSHR are underlined.