Assessing potentiation of the (α4) 3 (β2) 2 nicotinic acetylcholine receptor by the allosteric agonist CMPI
F Deba, K Munoz, E Peredia, G Akk… - Journal of Biological …, 2022 - ASBMB
The extracellular domain of the nicotinic acetylcholine receptor isoforms formed by three α4
and two β2 subunits ((α4) 3 (β2) 2 nAChR) harbors two high-affinity" canonical"
acetylcholine (ACh)-binding sites located in the two α4: β2 intersubunit interfaces and a low-
affinity" noncanonical" ACh-binding site located in the α4: α4 intersubunit interface. In this
study, we used ACh, cytisine, and nicotine (which bind at both the α4: α4 and α4: β2
interfaces), TC-2559 (which binds at the α4: β2 but not at the α4: α4 interface), and 3-(2 …
and two β2 subunits ((α4) 3 (β2) 2 nAChR) harbors two high-affinity" canonical"
acetylcholine (ACh)-binding sites located in the two α4: β2 intersubunit interfaces and a low-
affinity" noncanonical" ACh-binding site located in the α4: α4 intersubunit interface. In this
study, we used ACh, cytisine, and nicotine (which bind at both the α4: α4 and α4: β2
interfaces), TC-2559 (which binds at the α4: β2 but not at the α4: α4 interface), and 3-(2 …
以上显示的是最相近的搜索结果。 查看全部搜索结果