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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The ABCG2 multidrug transporter is a membrane protein from the ATP-binding cassette (ABC) transporter family, specifically the G-subfamily. Also know as the breast cancer resistance protein (BCRP), ABCG2 has physiological roles in various tissue cells including the mammary gland and the blood-brain, bloodtestis, and maternal-fetal barriers.[1] ABCG2 protects cells by exporting xenobiotic molecules out of the cell using ATP hydrolysis. ABCG2 also affects the pharmacokinetics of many drugs and contributes to multidrug resistance.[2]
Function
Transports xenobiotic molecules out of the cell (molecules that shouldn't be there) to protect cellular tissue (expand a bit/maybe combine intro and function?)
Structural highlights
Overall 3D Structure
ATP Bound and Unbound Conformations
FIGURE LEGEND
Cavities and Lysine Plug
Disease
Cancer
ABCG2 contributes to multidrug resistance in cancer cells by exporting anti-tumor drugs out of cells which is an obstacle in cancer treatment.[1]
brief description of the cancer genes listed in the papers (papers talk about how some cancers had more expression of abcg2 genes)
ABCG2 as a Target for Inhibition
Talk about how and why it would be a good target for the treatment of cancer
This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
↑ 1.01.1Cite error: Invalid <ref> tag; no text was provided for refs named Taylor
↑Cite error: Invalid <ref> tag; no text was provided for refs named Manolaridis
↑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:https://dx.doi.org/10.1038/nature22345
↑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:https://dx.doi.org/10.1038/s41586-018-0680-3