Summary for 7CF9
| Entry DOI | 10.2210/pdb7cf9/pdb |
| EMDB information | 30343 |
| Descriptor | Ryanodine receptor 1,RyR1, Peptidyl-prolyl cis-trans isomerase FKBP1B, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | rabbit, ryanodine receptor1, chl., membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 2208371.50 |
| Authors | Ma, R.,Haji-Ghassemi, O.,Ma, D.,Lin, L.,Samurkas, A.,Van Petegem, F.,Yuchi, Z. (deposition date: 2020-06-24, release date: 2020-09-02, Last modification date: 2024-03-27) |
| Primary citation | Ma, R.,Haji-Ghassemi, O.,Ma, D.,Jiang, H.,Lin, L.,Yao, L.,Samurkas, A.,Li, Y.,Wang, Y.,Cao, P.,Wu, S.,Zhang, Y.,Murayama, T.,Moussian, B.,Van Petegem, F.,Yuchi, Z. Structural basis for diamide modulation of ryanodine receptor. Nat.Chem.Biol., 16:1246-1254, 2020 Cited by PubMed Abstract: The diamide insecticide class is one of the top-selling insecticides globally. They are used to control a wide range of pests by targeting their ryanodine receptors (RyRs). Here, we report the highest-resolution cryo-electron microscopy (cryo-EM) structure of RyR1 in the open state, in complex with the anthranilic diamide chlorantraniliprole (CHL). The 3.2-Å local resolution map facilitates unambiguous assignment of the CHL binding site. The molecule induces a conformational change by affecting the S4-S5 linker, triggering channel opening. The binding site is further corroborated by mutagenesis data, which reveal how diamide insecticides are selective to the Lepidoptera group of insects over honeybee or mammalian RyRs. Our data reveal that several pests have developed resistance via two mechanisms, steric hindrance and loss of contact. Our results provide a foundation for the development of highly selective pesticides aimed at overcoming resistance and therapeutic molecules to treat human myopathies. PubMed: 32807966DOI: 10.1038/s41589-020-0627-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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