Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Conformational plasticity of human acid-sensing ion channel 1a.
Journal, issue, pages	Nat Struct Mol Biol, Year 2026
Publish date	Jul 16, 2026
Authors	James Cahill / Kimberly A Hartfield / Stephanie Andrea Heusser / Nadine Ritter / Mette Homann Poulsen / Craig Yoshioka / Stephan Alexander Pless / Isabelle Baconguis /
PubMed Abstract	Acid-sensing ion channels (ASICs) are typically activated by acidic environments and contribute to nociception and synaptic plasticity. ASIC1a is the most abundant subunit in the central nervous ...Acid-sensing ion channels (ASICs) are typically activated by acidic environments and contribute to nociception and synaptic plasticity. ASIC1a is the most abundant subunit in the central nervous system and forms homomeric channels permeable to Na and Ca, making it a compelling therapeutic target for acidotic pathologies including stroke and traumatic brain injury. However, a complete conformational library of human ASIC1a has yet to be described. Here we show that human ASIC1a adopts six major conformations, resolved by cryo-electron microscopy across a pH range between 8.5 and 5.7 and in the presence of a toxin agonist and a gating-modifying amino acid substitution. These major conformations establish linear transmembrane helices to be associated with an open state, delineate mechanistic differences between proton and toxin activation and demonstrate that desensitization involves unexpected conformational diversity in the transmembrane domain. Together, they provide a three-dimensional framework to integrate previous structure-function studies on ASIC.
External links	Nat Struct Mol Biol / PubMed:42463865
Methods	EM (single particle)
Resolution	2.33 - 3.41 Å
Structure data	47503 9e4a EMDB-47503, PDB-9e4a: Human ASIC1a at pH 8.5 with domain-swapped transmembrane domain Method: EM (single particle) / Resolution: 2.74 Å 47504 9e4b EMDB-47504, PDB-9e4b: Human ASIC1a at pH 7.5 with domain-swapped transmembrane domain Method: EM (single particle) / Resolution: 3.09 Å 47505 9e4c EMDB-47505, PDB-9e4c: Human ASIC1a at pH 7.5 with partial transmembrane domain Method: EM (single particle) / Resolution: 3.41 Å 47506 9e4d EMDB-47506, PDB-9e4d: Human ASIC1a at pH 7.5 with linear transmembrane domain Method: EM (single particle) / Resolution: 3.19 Å 47507 9e4e EMDB-47507, PDB-9e4e: Human ASIC1a at pH 6.5 with linear transmembrane domain Method: EM (single particle) / Resolution: 3.16 Å 47508 9e4f EMDB-47508, PDB-9e4f: Human ASIC1a at pH 5.7 with domain-swapped transmembrane domain Method: EM (single particle) / Resolution: 2.69 Å 47509 9e4g EMDB-47509, PDB-9e4g: Human ASIC1a at pH 5.7 with linear transmembrane domain Method: EM (single particle) / Resolution: 2.8 Å 47510 9e4h EMDB-47510, PDB-9e4h: Human ASIC1a at pH 5.7 with rotated, domain-swapped transmembrane domain Method: EM (single particle) / Resolution: 2.61 Å 47511 9e4i EMDB-47511, PDB-9e4i: Human ASIC1a at pH 7.5 in complex with MitTx Method: EM (single particle) / Resolution: 2.33 Å 47512 9e4j EMDB-47512, PDB-9e4j: Human ASIC1a at pH 6.5 in complex with MitTx Method: EM (single particle) / Resolution: 2.87 Å 47513 9e4k EMDB-47513, PDB-9e4k: Human ASIC1a at pH 8.5, T26V mutation Method: EM (single particle) / Resolution: 2.77 Å
Source	homo sapiens (human) micrurus tener tener (cobra)
Keywords	MEMBRANE PROTEIN / Ion channel / Trimer / Toxin