Abstract
Background The human genome contains 48 members of the ABC protein family. We focus on the multidrug resistance transporter P-glycoprotein (P-gp, ABCB1), which is expressed at the blood-brain-barrier, in intestine, kidney, liver and macrophages. The first structure of an ABC exporter was from Staphylococcus aureus and showed a twisted architecture. The same fold was observed in MsbA, mouse P-glycoprotein and the human mitochondrial ABCB10 transporter. Although ABC exporters have now been crystallized in several conformations, uncertainty remained with respect to the physiological conformation because they seem not to be fully compatible with all biochemical evidence.
Highlights
The human genome contains 48 members of the ABC protein family
Which conformation does the ABC transporter P-glycoprotein adopt in the physiological membrane environment?
We focus on the multidrug resistance transporter P-glycoprotein (P-gp, ABCB1), which is expressed at the blood-brain-barrier, in intestine, kidney, liver and macrophages
Summary
The human genome contains 48 members of the ABC protein family. We focus on the multidrug resistance transporter P-glycoprotein (P-gp, ABCB1), which is expressed at the blood-brain-barrier, in intestine, kidney, liver and macrophages. Which conformation does the ABC transporter P-glycoprotein adopt in the physiological membrane environment? Thomas Stockner1, Yaprak Dönmez1, Zahida Parveen2, Peter Chiba2* From 18th Scientific Symposium of the Austrian Pharmacological Society (APHAR).
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