Extended Data Fig. 6: ABCB4 and ABCB1 chimeras reveal important residues.
From: Structure of the human lipid exporter ABCB4 in a lipid environment
a, The different levels of protein extracted with DDM:CHS from pellets of experiments in Fig. 4d are indicated by luminescence units relative to wt-ABCB4. Main peak heights (peak around 20 min) were used to normalize results of the extrusion assays. b, The three positions mutated in the 3 M construct (V985M, H989Q and A990V) are shown in a model of the ATP-Mg2+ bound ABCB4 in stick representation, and residues within 4 Å are shown in line representation. c, Residues V985, H989 and A990 and nearby residues on TMH12, from the model of ABCB4 in the closed conformation, are shown with associated density contoured at a level of σ = 6.5 and carved at a distance of 2 Å from residues. d, Residue positions corresponding to those in (a) are shown on the previously published model of human-mouse chimeric ABCB1 bound to the inhibitor zosuquidar44, used for homology modelling, with density from the associated map contoured at a level of σ = 6.5 and carved at a distance of 2 Å from residues.
