7KS3

GluK2/K5 with L-Glu

Summary for 7KS3

• Entry DOI: 10.2210/pdb7ks3/pdb
• EMDB information: 23014 23015 23017
• Descriptor: Glutamate receptor ionotropic, kainate 5,Green fluorescent protein chimera, Glutamate receptor ionotropic, kainate 2 (2 entities in total)
• Functional Keywords: kainate receptor, ionotropic glutamate receptor, membrane protein, ligand-gated ion channel, signaling protein
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 4
• Total formula weight: 459316.86

Authors

Khanra, N.,Brown, P.M.G.E.,Perozzo, A.M.,Bowie, D.,Meyerson, J.R. (deposition date: 2020-11-20, release date: 2021-03-24, Last modification date: 2024-11-20)

Primary citation

Khanra, N.,Brown, P.M.,Perozzo, A.M.,Bowie, D.,Meyerson, J.
Architecture and structural dynamics of the heteromeric GluK2/K5 kainate receptor.
Elife, 10:-, 2021

PubMed Abstract: Kainate receptors (KARs) are L-glutamate-gated ion channels that regulate synaptic transmission and modulate neuronal circuits. KARs have strict assembly rules and primarily function as heteromeric receptors in the brain. A longstanding question is how KAR heteromer subunits organize and coordinate together to fulfill their signature physiological roles. Here we report structures of the GluK2/GluK5 heteromer in apo, antagonist-bound, and desensitized states. The receptor assembles with two copies of each subunit, ligand binding domains arranged as two heterodimers and GluK5 subunits proximal to the channel. Strikingly, during desensitization, GluK2, but not GluK5, subunits undergo major structural rearrangements to facilitate channel closure. We show how the large conformational differences between antagonist-bound and desensitized states are mediated by the linkers connecting the pore helices to the ligand binding domains. This work presents the first KAR heteromer structure, reveals how its subunits are organized, and resolves how the heteromer can accommodate functionally distinct closed channel structures.

PubMed: 33724189
DOI: 10.7554/eLife.66097

Experimental method

ELECTRON MICROSCOPY (5.8 Å)