Fig. 6: Mapping of cysteine cross-linking data onto the active SecR structure.
From: Structure and dynamics of the active Gs-coupled human secretin receptor
a Side view. Left panel, secretin peptide analog; Middle panel, agonist cross-linking pattern; Right panel, antagonist cross-linking pattern. b Magnified view looking into the SecR TM core. Left panel, agonist cross-linking pattern; Middle panel, antagonist cross-linking pattern; Right panel, secretin peptide analog. Peptides are displayed in ribbon format with x-stick representation of side chains, colored gray. The position of cysteine substitution is shown in colored cpk format (Cys7, dark blue; Cys6, purple; Cys5, red; Cys2, orange). The SecR is shown in ribbon format with the location of the cysteine mutants displayed in combination cpk and surface representation. Sites of cross-linking are colored according to the site of peptide substitution with dark shading for those with highest efficiency (>50% of the highest efficiency label) and those with intermediate efficiency (25–50% of the highest efficiency label) having light shading.
