This title appears in the Scientific Report :
2021
Please use the identifier:
http://hdl.handle.net/2128/28744 in citations.
Please use the identifier: http://dx.doi.org/10.1016/j.str.2021.05.013 in citations.
Evidence for a credit-card-swipe mechanism in the human PC floppase ABCB4
Evidence for a credit-card-swipe mechanism in the human PC floppase ABCB4
ABCB4 is described as an ATP-binding cassette (ABC) transporter that primarily transports lipids of the phosphatidylcholine (PC) family but is also capable of translocating a subset of typical multidrug-resistance-associated drugs. The high degree of amino acid identity of 76% for ABCB4 and ABCB1, w...
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Personal Name(s): | Prescher, Martin |
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Bonus, Michele / Stindt, Jan / Keitel-Anselmino, Verena / Smits, Sander H. J. / Gohlke, Holger / Schmitt, Lutz (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; IBI-7 Jülich Supercomputing Center; JSC John von Neumann - Institut für Computing; NIC Bioinformatik; IBG-4 |
Published in: | Structure, 29 (2021) 10, S. 1144-1155.e5 |
Imprint: |
Cambridge, Mass.
Cell Press
2021
|
DOI: |
10.1016/j.str.2021.05.013 |
Document Type: |
Journal Article |
Research Program: |
Forschergruppe Gohlke Domain-Specific Simulation & Data Life Cycle Labs (SDLs) and Research Groups Utilization of renewable carbon and energy sources and engineering of ecosystem functions Biological and environmental resources for sustainable use Computational Science and Mathematical Methods |
Link: |
Published on 2021-06-08. Available in OpenAccess from 2022-06-08. |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1016/j.str.2021.05.013 in citations.
ABCB4 is described as an ATP-binding cassette (ABC) transporter that primarily transports lipids of the phosphatidylcholine (PC) family but is also capable of translocating a subset of typical multidrug-resistance-associated drugs. The high degree of amino acid identity of 76% for ABCB4 and ABCB1, which is a prototype multidrug-resistance-mediating protein, results in ABCB4's second subset of substrates, which overlap with ABCB1's substrates. This often leads to incomplete annotations of ABCB4, in which it was described as exclusively PC-lipid specific. When the hydrophilic amino acids from ABCB4 are changed to the analogous but hydrophobic ones from ABCB1, the stimulation of ATPase activity by 1,2-dioleoyl-sn-glycero-3-phosphocholine, as a prime example of PC lipids, is strongly diminished, whereas the modulation capability of ABCB1 substrates remains unchanged. This indicates two distinct and autonomous substrate binding sites in ABCB4. |