Extended and Structurally Supported Insights into Extracellular Hormone Binding, Signal Transduction and Organization of the Thyrotropin Receptor
Figure 2
Amino acid sequences of hormone subtypes and specific receptor fragments.
A) Alignment of hormone subtype amino acid sequences with signal peptides (numbering with signal peptides throughout the manuscript). The α-subunits of hTSH, bTSH, hTSH analogue (TR1401, Trophogen Inc., Rockville, MD) and thyrostimulin are shown, together with the β-subunit sequences of hFSH, hLH and hCG. Residues are colored according to their biophysical properties: blue - positively charged, red - negatively charged, green - hydrophobic, orange - hydrophilic, magenta – histidine, brown – cysteine, black – proline, light green - aromatic residues). B) Comparison of the amino acid sequences of different GPHR subtypes and LGRs. Residues are presented from the cysteine-box 2 through the transmembrane helix 1. Specificities are highlighted, including the positions of CAMs and amino acids relevant to binding.