Sandbox Reserved 1611: Difference between revisions

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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]


Multidrug Transporter ABCG2 is a dimer that consists of two cavities seperated by a leucine plug. 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 the substrate and ATP are bound and in place. Its inter- and intra-disulfides 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 seperated by a leucine plug. 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 the substrate and ATP are bound and in place. Its inter- and intra-disulfides promote the release of the substrate from the cavity into the extracellular space.  


</StructureSection>
</StructureSection>

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