Sandbox Reserved 1606

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== Structural highlights ==
== Structural highlights ==
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ABCG2 is a homodimer with each dimer containing two domains, the nucleotide binding domain (NBD) and the transmembrane domain (TMD). The NDB is located inside of the cell and exposed to the cytosol while the TMD is embedded in the cell membrane and exposed to the extracellular space. [[Image:membrane domains.png|200 px|right|thumb|Figure 1. Domains of ABCG2 Multidrug transporter]]
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ABCG2 is a homodimer with each dimer containing two domains, the nucleotide binding domain (NBD) and the transmembrane domain (TMD) which are fused together as a single peptide chain.<ref name="Taylor"/> The NBD is located inside of the cell and exposed to the cytosol while the TMD is embedded in the cell membrane and exposed to the extracellular space. [[Image:membrane domains.png|200 px|right|thumb|Figure 1. Domains of ABCG2 Multidrug transporter]]
===ATP Bound and Unbound Conformations===
===ATP Bound and Unbound Conformations===
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 in order to cultivate the energy needed for the transport of molecules across the cell membrane. One molecule of <scene name='83/832932/Atp_bound_use/1'>ATP binds each NBD</scene> resulting in a conformational change of the overall ABCG2 structure.
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 in order to cultivate the energy needed for the transport of molecules across the cell membrane. One molecule of <scene name='83/832932/Atp_bound_use/1'>ATP binds each NBD</scene> resulting in a conformational change of the overall ABCG2 structure.

Revision as of 17:06, 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

ABCG2 Multidrug Transporter

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References

[1] [2]

  1. ↑ 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. ↑ 2.0 2.1 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

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