http://purl.uniprot.org/citations/32832629 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/32832629 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/32832629 | http://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/32832629 | http://purl.org/dc/terms/identifier | "doi:10.1126/sciadv.aba8105"xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.org/dc/terms/identifier | "doi:10.1126/sciadv.aba8105"xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Nomura K."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Nomura K."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Nishizawa T."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Nishizawa T."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Shimada H."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Shimada H."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Nureki O."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Nureki O."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Kusakizako T."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Kusakizako T."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Yamashita K."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Yamashita K."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Shihoya W."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Shihoya W."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Hiraizumi M."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Hiraizumi M."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Taruno A."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Taruno A."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Demura K."xsd:string |
http://purl.uniprot.org/citations/32832629 | http://purl.uniprot.org/core/author | "Demura K."xsd:string |