Kumari, J. and Vinnakota, R. and Kumar, J. (2019) Structural and Functional Insights intoGluK3-kainate Receptor Desensitization and Recovery. Scientific Reports , 9 (1).
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Abstract
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.
Item Type: | Article |
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Depositing User: | Mr. Rameshwar Nema |
Date Deposited: | 21 Feb 2020 05:58 |
Last Modified: | 08 Dec 2021 10:59 |
URI: | http://nccs.sciencecentral.in/id/eprint/734 |
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