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Crystal structure of the GluK3 ligand binding domain complex with SYM and zincCrystal structure of the GluK3 ligand binding domain complex with SYM and zinc
Structural highlights
Publication Abstract from PubMedGluK3-kainate receptors are atypical members of the iGluR family that reside at both the pre- and postsynapse and play a vital role in the regulation of synaptic transmission. For a better understanding of structural changes that underlie receptor functions, GluK3 receptors were trapped in desensitized and resting/closed states and structures analyzed using single particle cryo-electron microscopy. While the desensitized GluK3 has domain organization as seen earlier for another kainate receptor-GluK2, antagonist bound GluK3 trapped a resting state with only two LBD domains in dimeric arrangement necessary for receptor activation. Using structures as a guide, we show that the N-linked glycans at the interface of GluK3 ATD and LBD likely mediate inter-domain interactions and attune receptor-gating properties. The mutational analysis also identified putative N-glycan interacting residues. Our results provide a molecular framework for understanding gating properties unique to GluK3 and exploring the role of N-linked glycosylation in their modulation. Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery.,Kumari J, Vinnakota R, Kumar J Sci Rep. 2019 Jul 16;9(1):10254. doi: 10.1038/s41598-019-46770-z. PMID:31311973[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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