8YMX
The structure of BRTNaC1 at 40 degree centigrade
Summary for 8YMX
| Entry DOI | 10.2210/pdb8ymx/pdb |
| EMDB information | 39410 |
| Descriptor | Broad-range thermal receptor 1 (1 entity in total) |
| Functional Keywords | brtnac1, membrane protein, trimer |
| Biological source | Scolopendra mutilans |
| Total number of polymer chains | 3 |
| Total formula weight | 147931.02 |
| Authors | |
| Primary citation | Chen, X.,Yuan, L.,Wen, H.,Ma, Q.,Deng, Z.,Xu, Y.,Yao, Z.,Wang, Y.,Yang, S.,Su, N.,Yang, F. Structure and function of a broad-range thermal receptor in myriapods. Nat.Struct.Mol.Biol., 32:1081-1090, 2025 Cited by PubMed Abstract: Broad-range thermal receptor 1 (BRTNaC1), activated by heat at low extracellular pH, was recently identified in myriapods. Although the overexpression of BRTNaC1 leads to robust heat-activated current with a cation selectivity profile, the structure of this receptor and how it is gated by proton and heat remain to be investigated. Here we determine cryogenic electron microscopy structures of BRTNaC1 in the apo, proton-induced and heated states. Based on these structures, patch-clamp recordings and molecular dynamic simulations, we found that a 'twist the wrist' mechanism is used for proton activation of BRTNaC1, while heat induces broad conformational changes in BRTNaC1, including rotation and shift in the transmembrane helices to open this channel. Moreover, as testosterone inhibited BRTNaC1 activation, we identified four clustered residues important for such inhibition. Therefore, our study has established the structural basis for ligand and temperature gating in the BRTNaC1 ion channel. PubMed: 40011748DOI: 10.1038/s41594-025-01495-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.27 Å) |
Structure validation
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