7LVT

Structure of full-length GluK1 with L-Glu

Summary for 7LVT

• Entry DOI: 10.2210/pdb7lvt/pdb
• EMDB information: 23542
• Descriptor: Isoform Glur5-2 of Glutamate receptor ionotropic, kainate 1 (1 entity in total)
• Functional Keywords: ion channel, glutamate receptor, kainate receptor, membrane protein
• Biological source: Rattus norvegicus (Rat)
• Total number of polymer chains: 4
• Total formula weight: 410248.31

Authors

Meyerson, J.R.,Selvakumar, P. (deposition date: 2021-02-26, release date: 2021-11-03, Last modification date: 2024-10-09)

Primary citation

Selvakumar, P.,Lee, J.,Khanra, N.,He, C.,Munguba, H.,Kiese, L.,Broichhagen, J.,Reiner, A.,Levitz, J.,Meyerson, J.R.
Structural and compositional diversity in the kainate receptor family.
Cell Rep, 37:109891-109891, 2021

PubMed Abstract: The kainate receptors (KARs) are members of the ionotropic glutamate receptor family and assemble into tetramers from a pool of five subunit types (GluK1-5). Each subunit confers distinct functional properties to a receptor, but the compositional and stoichiometric diversity of KAR tetramers is not well understood. To address this, we first solve the structure of the GluK1 homomer, which enables a systematic assessment of structural compatibility among KAR subunits. Next, we analyze single-cell RNA sequencing data, which reveal extreme diversity in the combinations of two or more KAR subunits co-expressed within the same cell. We then investigate the composition of individual receptor complexes using single-molecule fluorescence techniques and find that di-heteromers assembled from GluK1, GluK2, or GluK3 can form with all possible stoichiometries, while GluK1/K5, GluK2/K5, and GluK3/K5 can form 3:1 or 2:2 complexes. Finally, using three-color single-molecule imaging, we discover that KARs can form tri- and tetra-heteromers.

PubMed: 34706237
DOI: 10.1016/j.celrep.2021.109891

Experimental method

ELECTRON MICROSCOPY (4.6 Å)