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Figure 1.
FIGURE 1. Structural sequence alignment of squid rhodopsin,
bovine rhodopsin and β[2]AR. The structural alignment was based
on the 3D-Coffee alignment (4). Residues on helix regions are
colored red, and residue(s) of helix bending are colored in
blue. Transmembrane helical regions (TH1–TH7) and helix H8
with extracellular (EL1–EL3) and cytoplasmic (CL1–CL3)
loops, and each helix in N- and C-terminal tails (NH and CH) are
indicated. Posttranslational modifications are shaded by the
following colors: cyan, N-glycosylation; a pair of pink or
green, disulfide bridge(s); yellow, palmitoylated cysteine;
blue, Schiff-based lysine with 11-cis-retinal; gold, N-terminal
methionine acetylation. Residues indicated by small letters are
not in models but in crystal protein samples, and residues
indicated by small letters in italic gray do not exist in the
crystal sample proteins due to expression processing, protease
digestion, or protein engineering. Squ_rhod, squid rhodopsin
(PDB code: 2ZIY in this study); Bov_rhod, bovine rhodopsin (1F88
(5) or 1GZM (17)); and ADRB2 (2RH1 (8)).
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