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http://purl.uniprot.org/citations/32832629http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32832629http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32832629http://www.w3.org/2000/01/rdf-schema#comment"Calcium homeostasis modulator (CALHM) family proteins are Ca2+-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we present the cryo-electron microscopy (EM) structures of killifish CALHM1, human CALHM2, and Caenorhabditis elegans CLHM-1 at resolutions of 2.66, 3.4, and 3.6 Å, respectively. The CALHM1 octamer structure reveals that the N-terminal helix forms the constriction site at the channel pore in the open state and modulates the ATP conductance. The CALHM2 undecamer and CLHM-1 nonamer structures show the different oligomeric stoichiometries among CALHM homologs. We further report the cryo-EM structures of the chimeric construct, revealing that the intersubunit interactions at the transmembrane domain (TMD) and the TMD-intracellular domain linker define the oligomeric stoichiometry. These findings advance our understanding of the ATP conduction and oligomerization mechanisms of CALHM channels."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.aba8105"xsd:string
http://purl.uniprot.org/citations/32832629http://purl.org/dc/terms/identifier"doi:10.1126/sciadv.aba8105"xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Nomura K."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Nomura K."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Nishizawa T."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Nishizawa T."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Shimada H."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Shimada H."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Nureki O."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Nureki O."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Kusakizako T."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Kusakizako T."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Yamashita K."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Yamashita K."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Shihoya W."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Shihoya W."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Hiraizumi M."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Hiraizumi M."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Taruno A."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Taruno A."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Demura K."xsd:string
http://purl.uniprot.org/citations/32832629http://purl.uniprot.org/core/author"Demura K."xsd:string