7cfs: Difference between revisions
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==Cryo-EM strucutre of human acid-sensing ion channel 1a at pH 8.0== | ==Cryo-EM strucutre of human acid-sensing ion channel 1a at pH 8.0== | ||
<StructureSection load='7cfs' size='340' side='right'caption='[[7cfs]]' scene=''> | <StructureSection load='7cfs' size='340' side='right'caption='[[7cfs]], [[Resolution|resolution]] 3.56Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CFS OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CFS FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.56Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cfs OCA], [https://pdbe.org/7cfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cfs RCSB], [https://www.ebi.ac.uk/pdbsum/7cfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cfs ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:32915133</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cfs" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 13:55, 23 October 2024
Cryo-EM strucutre of human acid-sensing ion channel 1a at pH 8.0Cryo-EM strucutre of human acid-sensing ion channel 1a at pH 8.0
Structural highlights
Publication Abstract from PubMedAcid-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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