Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure and desensitization of AMPA receptor complexes with type II TARP γ5 and GSG1L.
Journal, issue, pages	Mol Cell, Vol. 81, Issue 23, Page 4771-44783.e7, Year 2021
Publish date	Dec 2, 2021
Authors	Oleg Klykov / Shanti Pal Gangwar / Maria V Yelshanskaya / Laura Yen / Alexander I Sobolevsky /
PubMed Abstract	AMPA receptors (AMPARs) mediate the majority of excitatory neurotransmission. Their surface expression, trafficking, gating, and pharmacology are regulated by auxiliary subunits. Of the two types of ...AMPA receptors (AMPARs) mediate the majority of excitatory neurotransmission. Their surface expression, trafficking, gating, and pharmacology are regulated by auxiliary subunits. Of the two types of TARP auxiliary subunits, type I TARPs assume activating roles, while type II TARPs serve suppressive functions. We present cryo-EM structures of GluA2 AMPAR in complex with type II TARP γ5, which reduces steady-state currents, increases single-channel conductance, and slows recovery from desensitization. Regulation of AMPAR function depends on its ligand-binding domain (LBD) interaction with the γ5 head domain. GluA2-γ5 complex shows maximum stoichiometry of two TARPs per AMPAR tetramer, being different from type I TARPs but reminiscent of the auxiliary subunit GSG1L. Desensitization of both GluA2-GSG1L and GluA2-γ5 complexes is accompanied by rupture of LBD dimer interface, while GluA2-γ5 but not GluA2-GSG1L LBD dimers remain two-fold symmetric. Different structural architectures and desensitization mechanisms of complexes with auxiliary subunits endow AMPARs with broad functional capabilities.
External links	Mol Cell / PubMed:34678168 / PubMed Central
Methods	EM (single particle)
Resolution	3.3 - 4.4 Å
Structure data	24748 7ryy EMDB-24748, PDB-7ryy: Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist glutamate Method: EM (single particle) / Resolution: 4.4 Å 24749 7ryz EMDB-24749, PDB-7ryz: Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit GSG1L bound to agonist quisqualate Method: EM (single particle) / Resolution: 4.15 Å 24750 7rz4 EMDB-24750, PDB-7rz4: Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK 200775 Method: EM (single particle) / Resolution: 3.6 Å 24751 7rz5 EMDB-24751, PDB-7rz5: Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK 200775 Method: EM (single particle) / Resolution: 3.3 Å 24752 7rz6 EMDB-24752, PDB-7rz6: Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist glutamate Method: EM (single particle) / Resolution: 4.4 Å 24753 7rz7 EMDB-24753, PDB-7rz7: Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist Quisqualate Method: EM (single particle) / Resolution: 4.2 Å 24754 7rz8 EMDB-24754, PDB-7rz8: Structure of the complex of LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to agonist quisqualate Method: EM (single particle) / Resolution: 4.1 Å 24755 7rz9 EMDB-24755, PDB-7rz9: Structure of the complex of AMPA receptor GluA2 with auxiliary subunit GSG1L in the apo state Method: EM (single particle) / Resolution: 4.15 Å 24756 7rza EMDB-24756, PDB-7rza: Structure of the complex of AMPA receptor GluA2 with auxiliary subunit GSG1L bound to agonist quisqualate Method: EM (single particle) / Resolution: 4.26 Å
Chemicals	ChemComp-PCW: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipidYM ChemComp-GLU: GLUTAMIC ACID / Glutamic acid ChemComp-QUS: (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID / agonistYM / Quisqualic acid ChemComp-ZK1: {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / antagonist, medicationYM / Fanapanel ChemComp-NAG*: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine
Source	rattus norvegicus (Norway rat)
Keywords	MEMBRANE PROTEIN / AMPA receptor / ion channel / neurotransmission / synapse / TARP gamma-5 / GSG1L