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Structure paper

TitleChannel opening and gating mechanism in AMPA-subtype glutamate receptors.
Journal, issue, pagesNature, Vol. 549, Issue 7670, Page 60-65, Year 2017
Publish dateJul 24, 2017
AuthorsEdward C Twomey / Maria V Yelshanskaya / Robert A Grassucci / Joachim Frank / Alexander I Sobolevsky
External linksPubMed:28737760 / Publisher's page
KeywordsAnimals / Calcium Channels / Claudins / Cryoelectron Microscopy / GSG1L protein, mouse / HEK293 Cells / Humans / Hydrophobic and Hydrophilic Interactions / Ion Channel Gating / Mice / Models, Molecular / Protein Conformation / Protein Subunits / Rats / Receptors, AMPA / Synaptic Transmission / glutamate receptor ionotropic, AMPA 2 / TRANSPORT PROTEIN / Ion channel
MethodsEM (single particle)
Resolution4.2 - 6.8 A
Structure data

EMDB-8819:
GluA2 bound to antagonist ZK and GSG1L in digitonin, state 1

EMDB-8820:
GluA2 bound to antagonist ZK and GSG1L in digitonin, state 2

EMDB-8821:
GluA2 bound to GSG1L in digitonin, state 1

EMDB-8822:
GluA2 bound to GSG1L in digitonin, state 2

EMDB-8823:
Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin

PDB-5wek:
GluA2 bound to antagonist ZK and GSG1L in digitonin, state 1

PDB-5wel:
GluA2 bound to antagonist ZK and GSG1L in digitonin, state 2

PDB-5wem:
GluA2 bound to GSG1L in digitonin, state 1

PDB-5wen:
GluA2 bound to GSG1L in digitonin, state 2

PDB-5weo:
Activated GluA2 complex bound to glutamate, cyclothiazide, and STZ in digitonin

Chemicals

ChemComp-ZK1:
{[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid

ChemComp-AJP:
DigitoninDigitonin

ChemComp-GLU:
GLUTAMIC ACIDGlutamic acid

ChemComp-CYZ:
CYCLOTHIAZIDECyclothiazide

Source
  • Rattus norvegicus (Norway rat)
  • rattus norvegicus (Norway rat)
  • mus musculus (house mouse)

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