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As an [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC Transporter], ABCG2 exhibits ATPase activity in which the protein binds and hydrolyzes ATP. After the binding of a substrate, one molecule of <scene name='83/832932/Atp_bound_use2/1'>ATP binds each NBD</scene> causing a conformational change of the overall structure from an <scene name='83/832932/Overall_structure/2'>open conformation</scene> with no ATP bound to a <scene name='83/832932/Atp_bound_use/1'>closed conformation</scene>. One molecule of ATP is hydrolyzed to transport substrates across the cell membrane while second molecule of ATP is hydrolyzed to reset the transporter to its open conformation.<ref name="Robey"/> | As an [https://en.wikipedia.org/wiki/ATP-binding_cassette_transporter ABC Transporter], ABCG2 exhibits ATPase activity in which the protein binds and hydrolyzes ATP. After the binding of a substrate, one molecule of <scene name='83/832932/Atp_bound_use2/1'>ATP binds each NBD</scene> causing a conformational change of the overall structure from an <scene name='83/832932/Overall_structure/2'>open conformation</scene> with no ATP bound to a <scene name='83/832932/Atp_bound_use/1'>closed conformation</scene>. One molecule of ATP is hydrolyzed to transport substrates across the cell membrane while second molecule of ATP is hydrolyzed to reset the transporter to its open conformation.<ref name="Robey"/> | ||
| - | When ATP binds, α-helices in the NBD rotate approximately 35 degrees relative to their starting positions. This shift in the NBD causes slight shifts of α-helices in the TMD; these helices are pushed toward each other relative to their starting positions.The interface between the NBD and TMD | + | When ATP binds, α-helices in the NBD rotate approximately 35 degrees relative to their starting positions. This shift in the NBD causes slight shifts of α-helices in the TMD; these helices are pushed toward each other relative to their starting positions.The interface between the NBD and TMD remains largely unchanged. This overall shift in conformation promotes the transport of substrates through the transporter.<ref name="Manolaridis"/> |
Revision as of 22:35, 4 April 2020
| This Sandbox is Reserved from Jan 13 through September 1, 2020 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1598 through Sandbox Reserved 1627. |
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ABCG2 Multidrug Transporter
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References
- ↑ 1.0 1.1 1.2 1.3 Taylor NMI, Manolaridis I, Jackson SM, Kowal J, Stahlberg H, Locher KP. Structure of the human multidrug transporter ABCG2. Nature. 2017 Jun 22;546(7659):504-509. doi: 10.1038/nature22345. Epub 2017 May, 29. PMID:28554189 doi:http://dx.doi.org/10.1038/nature22345
- ↑ 2.0 2.1 2.2 Manolaridis I, Jackson SM, Taylor NMI, Kowal J, Stahlberg H, Locher KP. Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states. Nature. 2018 Nov;563(7731):426-430. doi: 10.1038/s41586-018-0680-3. Epub 2018 Nov, 7. PMID:30405239 doi:http://dx.doi.org/10.1038/s41586-018-0680-3
- ↑ 3.0 3.1 Robey RW, Pluchino KM, Hall MD, Fojo AT, Bates SE, Gottesman MM. Revisiting the role of ABC transporters in multidrug-resistant cancer. Nat Rev Cancer. 2018 Jul;18(7):452-464. doi: 10.1038/s41568-018-0005-8. PMID:29643473 doi:http://dx.doi.org/10.1038/s41568-018-0005-8
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