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. Author manuscript; available in PMC: 2012 Jul 25.
Published in final edited form as: Nat Chem Biol. 2011 Aug 21;7(10):692–700. doi: 10.1038/nchembio.634

Figure 4. Reactivities of residues in β2AR featuring conformational rearrangements of classic receptor activation.

Figure 4

(a,b) effects of nine β2AR ligands on neM reactivity at cys77 (a) and at cys327 (b). insets indicate position of labeled residue in the β2AR snake-like diagram. bar graphs depict the reactivity of each site with the different ligands bound to the β2AR, indicated on the y-axis by l-factor values relative to the value for receptor without ligand. bars extending below the x-axis indicate lower l-factors, and bars extending above it indicate higher l-factors relative to the receptor without ligand. All l-factors shown are for the fast phase. data correspond to the means ± standard errors of at least three independent experiments. Asterisks indicate statistical significance (*P < 0.05) compared to control receptor alone by one-way AnovA.