Sandbox Reserved 1611: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 17: | Line 17: | ||
[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 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. | ||
| Line 24: | Line 25: | ||
<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> | |||
<references/> | <references/> | ||
Revision as of 04:27, 24 March 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. |
To get started:
More help: Help:Editing |
Multidrug Transporter ABCG2 in Homo Sapiens
| ||||||||||||
References
- ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:https://dx.doi.org/10.1002/1873-3468.12677
- ↑ Jackson SM, Manolaridis I, Kowal J, Zechner M, Taylor NMI, Bause M, Bauer S, Bartholomaeus R, Bernhardt G, Koenig B, Buschauer A, Stahlberg H, Altmann KH, Locher KP. Structural basis of small-molecule inhibition of human multidrug transporter ABCG2. Nat Struct Mol Biol. 2018 Apr;25(4):333-340. doi: 10.1038/s41594-018-0049-1. Epub, 2018 Apr 2. PMID:29610494 doi:https://dx.doi.org/10.1038/s41594-018-0049-1
- ↑ 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:https://dx.doi.org/10.1038/s41586-018-0680-3
Student Contributors
- Shelby Skaggs
