| Home > Publications database > Evidence for a credit-card-swipe mechanism in the human PC floppase ABCB4 > print |
| 001 | 893209 | ||
| 005 | 20230111074309.0 | ||
| 024 | 7 | _ | |a 10.1016/j.str.2021.05.013 |2 doi |
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| 100 | 1 | _ | |a Prescher, Martin |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Evidence for a credit-card-swipe mechanism in the human PC floppase ABCB4 |
| 260 | _ | _ | |a Cambridge, Mass. |c 2021 |b Cell Press |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Stindt, Jan |0 0000-0002-8760-1989 |b 2 |
| 700 | 1 | _ | |a Keitel-Anselmino, Verena |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Smits, Sander H. J. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Gohlke, Holger |0 P:(DE-Juel1)172663 |b 5 |u fzj |
| 700 | 1 | _ | |a Schmitt, Lutz |0 P:(DE-HGF)0 |b 6 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.str.2021.05.013 |g p. S0969212621001714 |0 PERI:(DE-600)2031189-8 |n 10 |p 1144-1155.e5 |t Structure |v 29 |y 2021 |x 0969-2126 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/893209/files/Manuscript_modified_MP_HG.pdf |y Published on 2021-06-08. Available in OpenAccess from 2022-06-08. |
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