{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhou C"],"funding":["Whitehall Foundation (Whitehall Foundation, Inc.)","U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS)","NIGMS NIH HHS"],"pagination":["10989"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12690123"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Kainate receptors (KARs) belong to the ionotropic glutamate receptor (iGluR) family and play critical roles in mediating excitatory neurotransmission and regulating neurotransmitter release. Receptor desensitization is a critical factor for regulating the strength of synaptic transmission. Notwithstanding their overall structural similarity to AMPA receptors, KARs exhibit a desensitized conformation that is distinct from that of most other iGluRs. Despite extensive studies on KARs, a fundamental question remains unresolved: why do KARs require large conformational changes upon desensitization? Here we show cryo-electron microscopy structures of GluK2 containing double cysteine mutations, captured in non-active and various desensitized conformations. In the shallow-desensitized conformation"],"journal":["Nature communications"],"pubmed_title":["Structural insights into kainate receptor desensitization."],"pmcid":["PMC12690123"],"funding_grant_id":["R35 GM147266","1R35GM147266-01","2022-05-080"],"pubmed_authors":["Segura-Covarrubias G","Tajima N","Zhou C"],"additional_accession":[]},"is_claimable":false,"name":"Structural insights into kainate receptor desensitization.","description":"Kainate receptors (KARs) belong to the ionotropic glutamate receptor (iGluR) family and play critical roles in mediating excitatory neurotransmission and regulating neurotransmitter release. Receptor desensitization is a critical factor for regulating the strength of synaptic transmission. Notwithstanding their overall structural similarity to AMPA receptors, KARs exhibit a desensitized conformation that is distinct from that of most other iGluRs. Despite extensive studies on KARs, a fundamental question remains unresolved: why do KARs require large conformational changes upon desensitization? Here we show cryo-electron microscopy structures of GluK2 containing double cysteine mutations, captured in non-active and various desensitized conformations. In the shallow-desensitized conformation","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-06T03:54:09.159Z","creation":"2026-05-25T03:12:17.869Z"},"accession":"S-EPMC12690123","cross_references":{"pubmed":["41365859"],"doi":["10.1038/s41467-025-65920-8"]}}