6JFY
GluK3 receptor trapped in Desensitized state
Summary for 6JFY
| Entry DOI | 10.2210/pdb6jfy/pdb |
| EMDB information | 9821 |
| Descriptor | Glutamate receptor ionotropic, kainate 3 (1 entity in total) |
| Functional Keywords | glutamate receptor, kainate, sym, membrane protein |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 4 |
| Total formula weight | 365223.25 |
| Authors | Kumari, J.,Kumar, J. (deposition date: 2019-02-13, release date: 2019-07-24, Last modification date: 2024-11-20) |
| Primary citation | Kumari, J.,Vinnakota, R.,Kumar, J. Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery. Sci Rep, 9:10254-10254, 2019 Cited by PubMed 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. PubMed: 31311973DOI: 10.1038/s41598-019-46770-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.4 Å) |
Structure validation
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