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== Introduction ==
== Introduction ==


== Function ==
== Function ==
[https://www-sciencedirect-com.ezproxy.butler.edu/science/article/pii/S0304383505003538]


ABCG2 transports a variety of substrates, particularly flat, hydrophobic, and/or polycylic molecules. It is found in different biological membranes, such as the blood-brain barrier (BBB), blood-testis barrier, and the blood-placental barrier. It is thought to help protect those tissues and many others from cytotoxins. In addition to cytotoxin protection, ABCG2 secretes endogenous substrates in the adrenal gland, excretes toxins in the liver and kidneys, and regulates absorption of substrates.
== Disease ==
== Disease ==


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[https://www.nature.com/articles/s41594-018-0049-1 Nature_Structural_&_Molecular_Biology_Vol_25]
[https://www.nature.com/articles/s41594-018-0049-1 Nature_Structural_&_Molecular_Biology_Vol_25]
[https://www.nature.com/articles/s41586-018-0680-3]


Multidrug Transporter ABCG2 is a <scene name='83/832937/Dimer/1'>dimer</scene> that consists of two cavities seperated by a <scene name='83/832937/Leucine_plug/1'>leucine plug</scene>. Cavity 1 is a binding pocket open to the cytoplasm and the inner leaflet of the plasma membrane. Its shape is suitable to bind flat, hydrophobic and polycyclic substrates. Many of its amino acids residues form hydrophobic interactions with the bound substrate, as shown in green in '''Figure 1'''.  Cavity 2 is located above the leucine plug. It is empty until a <scene name='83/832937/Atp_and_mg_bound_to_abcg2/2'>magnesium ion and ATP</scene> are bound to ABCG2. Its <scene name='83/832937/Cysteine_disulfide_bridges/2'>inter- and intra-disulfides</scene> promote the release of the substrate from the cavity into the extracellular space.  
Multidrug Transporter ABCG2 is a <scene name='83/832937/Dimer/1'>dimer</scene> that consists of two cavities separated by a <scene name='83/832937/Leucine_plug/4'>leucine plug</scene>. Cavity 1 is a binding pocket open to the cytoplasm and the inner leaflet of the plasma membrane. Its shape is suitable to bind flat, hydrophobic and polycyclic substrates. Many of its amino acids residues form hydrophobic interactions with the bound substrate, as shown in green in '''Figure 1'''.  Cavity 2 is located above the leucine plug. It is empty until a <scene name='83/832937/Atp_and_mg_bound_to_abcg2/4'>magnesium ion and ATP</scene> are bound to ABCG2. <scene name='83/832937/Cysteine_disulfide_bridges/5'>inter- and intra-disulfides</scene> promote the release of the substrate from the cavity into the extracellular space.  


</StructureSection>
</StructureSection>
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<ref name="Ransey">PMID:28504306</ref>
<ref name="Ransey">PMID:28504306</ref>
<ref name="Jackson">PMID:29610494</ref>
<ref name="Jackson">PMID:29610494</ref>
<ref name="Manolaridis">PMID:30405239</ref>
<ref name="Fetsch">PMID:15990223</ref>
<references/>
<references/>


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OCA, Shelby Skaggs