7SMT
Cryo-EM structure of Torpedo acetylcholine receptor in complex with d-tubocurarine and carbachol
Summary for 7SMT
| Entry DOI | 10.2210/pdb7smt/pdb |
| EMDB information | 25202 25205 25206 25207 25208 |
| Descriptor | Acetylcholine receptor subunit alpha, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total) |
| Functional Keywords | acetylcholine receptor, nicotinic receptor, torpedo, cys-loop receptor, ion channel, muscle-type nicotinic receptor, transport protein |
| Biological source | Tetronarce californica (Pacific electric ray) More |
| Total number of polymer chains | 5 |
| Total formula weight | 278061.86 |
| Authors | Rahman, M.M.,Basta, T.,Teng, J.,Lee, M.,Worrell, B.T.,Stowell, M.H.B.,Hibbs, R.E. (deposition date: 2021-10-26, release date: 2022-03-09, Last modification date: 2024-10-16) |
| Primary citation | Rahman, M.M.,Basta, T.,Teng, J.,Lee, M.,Worrell, B.T.,Stowell, M.H.B.,Hibbs, R.E. Structural mechanism of muscle nicotinic receptor desensitization and block by curare. Nat.Struct.Mol.Biol., 29:386-394, 2022 Cited by PubMed Abstract: Binding of the neurotransmitter acetylcholine to its receptors on muscle fibers depolarizes the membrane and thereby triggers muscle contraction. We sought to understand at the level of three-dimensional structure how agonists and antagonists alter nicotinic acetylcholine receptor conformation. We used the muscle-type receptor from the Torpedo ray to first define the structure of the receptor in a resting, activatable state. We then determined the receptor structure bound to the agonist carbachol, which stabilizes an asymmetric, closed channel desensitized state. We find conformational changes in a peripheral membrane helix are tied to recovery from desensitization. To probe mechanisms of antagonism, we obtained receptor structures with the active component of curare, a poison arrow toxin and precursor to modern muscle relaxants. d-Tubocurarine stabilizes the receptor in a desensitized-like state in the presence and absence of agonist. These findings define the transitions between resting and desensitized states and reveal divergent means by which antagonists block channel activity of the muscle-type nicotinic receptor. PubMed: 35301478DOI: 10.1038/s41594-022-00737-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.56 Å) |
Structure validation
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