Fig. 1: Conformational dynamics of tβ1AR upon binding to antagonist. | Nature Communications

Fig. 1: Conformational dynamics of tβ1AR upon binding to antagonist.

From: Ligand-induced conformational changes in the β1-adrenergic receptor revealed by hydrogen-deuterium exchange mass spectrometry

Fig. 1

A Chemical structure of antagonist carvedilol, ΔHDX-MS results for tβ1AR + carvedilol vs tβ1AR mapped on β1AR structure, deuterium uptake plots for ICL1 and TM5. B Chemical structure of antagonist carazolol, ΔHDX-MS results for tβ1AR + carazolol vs tβ1AR. C Chemical structure of antagonist cyanopindolol, ΔHDX-MS results for tβ1AR + cyanopindolol vs tβ1AR. Results are mapped on tβ1AR structure (modelled using PDB structures; 2VT4 chain A and 6IBL chain A). Ser residues, crucial for binding the ligands into catecholamine binding pocket of the receptor, are highlighted in red. Relative deuterium uptake shows cumulative data across all time points for every receptor-ligand complex. Data are presented as mean values ± SD, where error bars represent the standard deviation at each time point. Each measurement is based on three technical replicates (n = 3). Source data are provided as a Source Data file.

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