@article {1159,
	title = {Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery [National Cryo-Electron Microscopy Facility]},
	journal = {Sci Rep},
	volume = {9},
	year = {2019},
	month = {2019 Jul 16},
	pages = {10254},
	abstract = {<p>GluK3-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.</p>
},
	issn = {2045-2322},
	doi = {10.1038/s41598-019-46770-z},
	author = {Kumari, Jyoti and Vinnakota, Rajesh and Kumar, Janesh}
}
