7cfs

Cryo-EM strucutre of human acid-sensing ion channel 1a at pH 8.0

spinqualitylabelsall models 7cfs, resolution 3.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.56Å Ligands: NA, NAG, Y01 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Acid-sensing ion channels (ASICs) are proton-gated cation channels that are involved in diverse neuronal processes including pain sensing. The peptide toxin Mambalgin1 (Mamba1) from black mamba snake venom can reversibly inhibit the conductance of ASICs, causing an analgesic effect. However, the detailed mechanism by which Mamba1 inhibits ASIC1s, especially how Mamba1 binding to the extracellular domain affects the conformational changes of the transmembrane domain of ASICs remains elusive. Here, we present single-particle cryo-EM structures of human ASIC1a (hASIC1a) and the hASIC1a-Mamba1 complex at resolutions of 3.56 and 3.90 A, respectively. The structures revealed the inhibited conformation of hASIC1a upon Mamba1 binding. The combination of the structural and physiological data indicates that Mamba1 preferentially binds hASIC1a in a closed state and reduces the proton sensitivity of the channel, representing a closed-state trapping mechanism. Structural insights into human acid-sensing ion channel 1a inhibition by snake toxin mambalgin1.,Sun D, Liu S, Li S, Zhang M, Yang F, Wen M, Shi P, Wang T, Pan M, Chang S, Zhang X, Zhang L, Tian C, Liu L Elife. 2020 Sep 11;9. pii: 57096. doi: 10.7554/eLife.57096. PMID:32915133 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA