Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6GIV

Structure of GluA2-N775S ligand-binding domain (S1S2J) in complex with glutamate and Rubidium Bromide at 1.75 A resolution

Summary for 6GIV
Entry DOI10.2210/pdb6giv/pdb
DescriptorGlutamate receptor 2, GLUTAMIC ACID, SULFATE ION, ... (6 entities in total)
Functional Keywordsionotropic glutamate receptor, glua2-n775s ligand-binding domain, agonist, membrane protein, bromide ions
Biological sourceRattus norvegicus (Norway Rat)
More
Total number of polymer chains1
Total formula weight29851.09
Authors
Venskutonyte, R.,Frydenvang, K.,Kastrup, J.S. (deposition date: 2018-05-15, release date: 2019-05-15, Last modification date: 2024-11-20)
Primary citationDawe, G.B.,Kadir, M.F.,Venskutonyte, R.,Perozzo, A.M.,Yan, Y.,Alexander, R.P.D.,Navarrete, C.,Santander, E.A.,Arsenault, M.,Fuentes, C.,Aurousseau, M.R.P.,Frydenvang, K.,Barrera, N.P.,Kastrup, J.S.,Edwardson, J.M.,Bowie, D.
Nanoscale Mobility of the Apo State and TARP Stoichiometry Dictate the Gating Behavior of Alternatively Spliced AMPA Receptors.
Neuron, 102:976-, 2019
Cited by
PubMed Abstract: Neurotransmitter-gated ion channels are allosteric proteins that switch on and off in response to agonist binding. Most studies have focused on the agonist-bound, activated channel while assigning a lesser role to the apo or resting state. Here, we show that nanoscale mobility of resting α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type ionotropic glutamate receptors (AMPA receptors) predetermines responsiveness to neurotransmitter, allosteric anions and TARP auxiliary subunits. Mobility at rest is regulated by alternative splicing of the flip/flop cassette of the ligand-binding domain, which controls motions in the distant AMPA receptor N-terminal domain (NTD). Flip variants promote moderate NTD movement, which establishes slower channel desensitization and robust regulation by anions and auxiliary subunits. In contrast, greater NTD mobility imparted by the flop cassette acts as a master switch to override allosteric regulation. In AMPA receptor heteromers, TARP stoichiometry further modifies these actions of the flip/flop cassette generating two functionally distinct classes of partially and fully TARPed receptors typical of cerebellar stellate and Purkinje cells.
PubMed: 31053408
DOI: 10.1016/j.neuron.2019.03.046
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon