6qkc

GluA1/2 In complex with auxiliary subunit gamma-8GluA1/2 In complex with auxiliary subunit gamma-8

6qkc, resolution 4.40Å Show:Asymmetric Unit Biological Assembly Structural highlights 6qkc is a 6 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.4Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GRIA1_RAT Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Publication Abstract from PubMed AMPA-type glutamate receptors (AMPARs) mediate excitatory neurotransmission, and are central regulators of synaptic plasticity, a molecular mechanism underlying learning and memory. Although AMPARs act predominantly as heteromers, structural studies have focused on homomeric assemblies. Here we present a cryo-EM structure of the heteromeric GluA1/2 receptor associated with two TARP gamma8 auxiliary subunits, the principle AMPAR complex at hippocampal synapses. Within the receptor, the core subunits arrange to give the GluA2 subunit dominant control of gating. This structure reveals the geometry of the Q/R-site controlling calcium flux, suggests association of TARP-stabilized lipids, and demonstrates that the extracellular loop of gamma8 modulates gating by selectively interacting with the GluA2 ligand-binding domain. Collectively, this structure provides a blueprint for deciphering the signal transduction mechanisms of synaptic AMPARs. Architecture of the heteromeric GluA1/2 AMPA receptor in complex with the auxiliary subunit TARP gamma8.,Herguedas B, Watson JF, Ho H, Cais O, Garcia-Nafria J, Greger IH Science. 2019 Mar 14. pii: science.aav9011. doi: 10.1126/science.aav9011. PMID:30872532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutamate receptor 3D structures Ion channels 3D structures