6WJC
Muscarinic acetylcholine receptor 1 - muscarinic toxin 7 complex
Summary for 6WJC
| Entry DOI | 10.2210/pdb6wjc/pdb |
| Descriptor | Muscarinic acetylcholine receptor M1,Endolysin fusion, Muscarinic toxin 7, ACETAMIDE, ... (6 entities in total) |
| Functional Keywords | gpcr, natural toxin, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 66990.36 |
| Authors | Maeda, S.,Kobilka, B.K. (deposition date: 2020-04-13, release date: 2020-07-08, Last modification date: 2024-11-13) |
| Primary citation | Maeda, S.,Xu, J.,N Kadji, F.M.,Clark, M.J.,Zhao, J.,Tsutsumi, N.,Aoki, J.,Sunahara, R.K.,Inoue, A.,Garcia, K.C.,Kobilka, B.K. Structure and selectivity engineering of the M1muscarinic receptor toxin complex. Science, 369:161-167, 2020 Cited by PubMed Abstract: Muscarinic toxins (MTs) are natural toxins produced by mamba snakes that primarily bind to muscarinic acetylcholine receptors (MAChRs) and modulate their function. Despite their similar primary and tertiary structures, MTs show distinct binding selectivity toward different MAChRs. The molecular details of how MTs distinguish MAChRs are not well understood. Here, we present the crystal structure of MAChR in complex with MT7, a subtype-selective anti-MAChR snake venom toxin. The structure reveals the molecular basis of the extreme subtype specificity of MT7 for MAChR and the mechanism by which it regulates receptor function. Through in vitro engineering of MT7 finger regions that was guided by the structure, we have converted the selectivity from MAChR toward MAChR, suggesting that the three-finger fold is a promising scaffold for developing G protein-coupled receptor modulators. PubMed: 32646996DOI: 10.1126/science.aax2517 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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