6QKZ

Full length GluA1/2-gamma8 complex

Summary for 6QKZ

• Entry DOI: 10.2210/pdb6qkz/pdb
• Related: 6QKC
• EMDB information: 4572 4575
• Descriptor: GluA1, Glutamate receptor 2, Voltage-dependent calcium channel gamma-8 subunit, ... (7 entities in total)
• Functional Keywords: ampar, ion channel, glua1, glua2, tarp, membrane protein
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 6
• Total formula weight: 481930.40

Authors

Herguedas, B.,Garcia-Nafria, J.,Greger, I.G. (deposition date: 2019-01-30, release date: 2019-03-27, Last modification date: 2020-07-29)

Primary citation

Herguedas, B.,Watson, J.F.,Ho, H.,Cais, O.,Garcia-Nafria, J.,Greger, I.H.
Architecture of the heteromeric GluA1/2 AMPA receptor in complex with the auxiliary subunit TARP gamma 8.
Science, 364:-, 2019

PubMed Abstract: 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-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) γ8 auxiliary subunits, the principal 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 that controls calcium flux, suggests association of TARP-stabilized lipids, and demonstrates that the extracellular loop of γ8 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.

PubMed: 30872532
DOI: 10.1126/science.aav9011

Experimental method

ELECTRON MICROSCOPY (6.3 Å)