6PV8
Human alpha3beta4 nicotinic acetylcholine receptor in complex with AT-1001
Summary for 6PV8
| Entry DOI | 10.2210/pdb6pv8/pdb |
| EMDB information | 20488 |
| Descriptor | Fusion protein of Neuronal acetylcholine receptor subunit alpha-3 and Soluble cytochrome b562, 2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (12 entities in total) |
| Functional Keywords | ligand-gated ion channel, nicotinic acetylcholine receptor, cys-loop receptor, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 9 |
| Total formula weight | 411781.86 |
| Authors | Gharpure, A.,Teng, J.,Zhuang, Y.,Noviello, C.M.,Walsh, R.M.,Cabuco, R.,Howard, R.J.,Zaveri, N.T.,Lindahl, E.,Hibbs, R.E. (deposition date: 2019-07-19, release date: 2019-09-11, Last modification date: 2024-11-20) |
| Primary citation | Gharpure, A.,Teng, J.,Zhuang, Y.,Noviello, C.M.,Walsh Jr., R.M.,Cabuco, R.,Howard, R.J.,Zaveri, N.T.,Lindahl, E.,Hibbs, R.E. Agonist Selectivity and Ion Permeation in the alpha 3 beta 4 Ganglionic Nicotinic Receptor. Neuron, 104:501-, 2019 Cited by PubMed Abstract: Nicotinic acetylcholine receptors are pentameric ion channels that mediate fast chemical neurotransmission. The α3β4 nicotinic receptor subtype forms the principal relay between the central and peripheral nervous systems in the autonomic ganglia. This receptor is also expressed focally in brain areas that affect reward circuits and addiction. Here, we present structures of the α3β4 nicotinic receptor in lipidic and detergent environments, using functional reconstitution to define lipids appropriate for structural analysis. The structures of the receptor in complex with nicotine, as well as the α3β4-selective ligand AT-1001, complemented by molecular dynamics, suggest principles of agonist selectivity. The structures further reveal much of the architecture of the intracellular domain, where mutagenesis experiments and simulations define residues governing ion conductance. PubMed: 31488329DOI: 10.1016/j.neuron.2019.07.030 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.87 Å) |
Structure validation
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