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

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