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.

Vadakkadath Meethal et al. BMC Evolutionary Biology 2006 6:103   doi:10.1186/1471-2148-6-103