ABCG2 multidrug transporter: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 18: | Line 18: | ||
When ATP binds, α-helices in the NBD <scene name='83/832932/Atp_bound_nbd/3'>rotate</scene> approximately 35° relative to the <scene name='83/832932/Overall_structure_nbd_unbound/5'>inward-facing conformation of NBD</scene>. This shift in the NBD causes slight shifts of α-helices in the TMD; these helices are <scene name='83/832932/Atp_bound_use_tmd/4'>pushed toward each other</scene> relative to the <scene name='83/832932/Overall_structure_tmd_unbound/4'>inward-facing conformation of TMD</scene>. The overall shift from inward-facing to outward-facing promotes the transport of substrates through the transporter.<ref name="Manolaridis"/> | When ATP binds, α-helices in the NBD <scene name='83/832932/Atp_bound_nbd/3'>rotate</scene> approximately 35° relative to the <scene name='83/832932/Overall_structure_nbd_unbound/5'>inward-facing conformation of NBD</scene>. This shift in the NBD causes slight shifts of α-helices in the TMD; these helices are <scene name='83/832932/Atp_bound_use_tmd/4'>pushed toward each other</scene> relative to the <scene name='83/832932/Overall_structure_tmd_unbound/4'>inward-facing conformation of TMD</scene>. The overall shift from inward-facing to outward-facing promotes the transport of substrates through the transporter.<ref name="Manolaridis"/> | ||
How the movement of the NBDs is linked to the movement of the transdomain movements is nicely visible in this <scene name='86/869419/Animation/2'>superposition</scene>.{{Template:Button Toggle Animation2}} | |||
The NBDs in ABCG2 remain in contact with one another even without a bound substrate, providing greater substrate specificity as the entrance to the transporter is not as globular as other ABC transporters like ABCB1 or ABCC1. The entrance from the cytoplasm to the transporter is lined by [https://en.wikipedia.org/wiki/Hydrophobe hydrophobic] residues<scene name='83/832939/Lining_of_entrance_of_nbd/1'> A397, V401, L405, L539, I543 and T547</scene> in both [https://en.wikipedia.org/wiki/Monomer monomers]. | The NBDs in ABCG2 remain in contact with one another even without a bound substrate, providing greater substrate specificity as the entrance to the transporter is not as globular as other ABC transporters like ABCB1 or ABCC1. The entrance from the cytoplasm to the transporter is lined by [https://en.wikipedia.org/wiki/Hydrophobe hydrophobic] residues<scene name='83/832939/Lining_of_entrance_of_nbd/1'> A397, V401, L405, L539, I543 and T547</scene> in both [https://en.wikipedia.org/wiki/Monomer monomers]. | ||