6JFZ

GluK3 receptor complex with UBP310

6JFZ の概要

• エントリーDOI: 10.2210/pdb6jfz/pdb
• EMDBエントリー: 9821 9822
• 分子名称: Glutamate receptor ionotropic, kainate 3 (1 entity in total)
• 機能のキーワード: glutamate receptor, kainate, ubp310, membrane protein
• 由来する生物種: Rattus norvegicus (Rat)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 365223.25

構造登録者

Kumari, J.,Kumar, J. (登録日: 2019-02-13, 公開日: 2019-07-24, 最終更新日: 2024-11-13)

主引用文献

Kumari, J.,Vinnakota, R.,Kumar, J.
Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery.
Sci Rep, 9:10254-10254, 2019

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: 31311973
DOI: 10.1038/s41598-019-46770-z

実験手法

ELECTRON MICROSCOPY (7.6 Å)