Table 2.
Conservation of functionally important amino acid residues (FIRs).
| Functional Site Type (# of residues) | Ce-GnRHR vs. human GnRHR1 | Ce-GnRHR vs. Dm-AKHR | Human GnRHR1 vs. Dm-AKHR | Ce-GnRHR vs. human Rhodopsin | Ce-GnRHR vs. human Vasopressin receptor |
| Receptor activation (6) | 83.3% | 83.3% | 83.3% | 75.0% | 83.3% |
| Ligand binding (7) | 35.7% | 21.4% | 42.9% | 7.1% | 35.7% |
| Binding pocket formation (24) | 54.2% | 68.8% | 72.9% | 43.8% | 33.3% |
| PKC phosphorylation (2) | 50.0% | 75.0% | 50.0% | 25.0% | 50.0% |
| Gq/11 G-protein coupling (8) | 62.5% | 93.8% | 68.8% | 56.2% | 62.5% |
| Gs G-protein coupling (3) | 50.0% | 33.3% | 33.3% | 0.0% | 33.3% |
| Total similarity (FIRs only) | 56.0% | 66.0% | 66.0% | 41.0% | 44.0% |
| Identity (all residues) | 20.8% | 26.6% | 20.4% | 12.4% | 17.9% |
| Identity + Similarity (all residues) | 36.3% | 45.2% | 37.9% | 28.5% | 34.4% |
Shown are the amino acid similarities between the functionally important residues of Ce-GnRHR and human GnRHR1, Drosophila melanogaster AKHR (Dm-AKHR), human rhodopsin, and human vasopressin type 1a. Also shown are the overall amino acid identity/similarity for each comparison. 'Similarity' of compared amino acids was based on the BLOSUM62 matrix, a more conservative measure of similarity than that used in the ALIGN algorithm, and percentages were calculated as described in methods.