Figure 3.

Sequence alignment of human MT1, MT2 and GPR50 with bovine rhodopsin (pdb 1F88). Sequence identities are reported white on a black background, whereas sequence similarities are boxed (A). The positions of the transmembrane helices, as observed in the bovine rhodopsin structure, are reported above its sequence. Arrows indicate the positions of the amino acids that, in GPR50, evolved under positive selection. Stars indicate amino acids which have been shown to play a key role for melatonin binding in MT1 (dark blue), MT2 (light blue) or both (red). A ribbon representation of the GPR50 3D structure model is represented (B), with transmembrane helices colored according to the sequence alignment. Amino acids evolving under positive selection and amino acids important for melatonin binding in MT1/MT2 are shown according to the colors reported in the sequence alignment.

Dufourny et al. BMC Evolutionary Biology 2012 12:28   doi:10.1186/1471-2148-12-28
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