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TitleStructural Basis of the Proton Sensitivity of Human GluN1-GluN2A NMDA Receptors.
Journal, issue, pagesCell Rep, Vol. 25, Issue 13, Page 3582-33590.e4, Year 2018
Publish dateDec 26, 2018
AuthorsJin-Bao Zhang / Shenghai Chang / Pan Xu / Miao Miao / Hangjun Wu / Youyi Zhang / Tongtong Zhang / Han Wang / Jilin Zhang / Chun Xie / Nan Song / Cheng Luo / Xing Zhang / Shujia Zhu /
PubMed AbstractN-methyl-D-aspartate (NMDA) receptors are critical for synaptic development and plasticity. While glutamate is the primary agonist, protons can modulate NMDA receptor activity at synapses during ...N-methyl-D-aspartate (NMDA) receptors are critical for synaptic development and plasticity. While glutamate is the primary agonist, protons can modulate NMDA receptor activity at synapses during vesicle exocytosis by mechanisms that are unknown. We used cryo-electron microscopy to solve the structures of the human GluN1-GluN2A NMDA receptor at pH 7.8 and pH 6.3. Our structures demonstrate that the proton sensor predominantly resides in the N-terminal domain (NTD) of the GluN2A subunit and reveal the allosteric coupling mechanism between the proton sensor and the channel gate. Under high-pH conditions, the GluN2A-NTD adopts an "open-and-twisted" conformation. However, upon protonation at the lower pH, the GluN2A-NTD transits from an open- to closed-cleft conformation, causing rearrangements between the tetrameric NTDs and agonist-binding domains. The conformational mobility observed in our structures (presumably from protonation) is supported by molecular dynamics simulation. Our findings reveal the structural mechanisms by which protons allosterically inhibit human GluN1-GluN2A receptor activity.
External linksCell Rep / PubMed:30590034
MethodsEM (single particle)
Resolution4.5 - 7.8 Å
Structure data

9714

6ira

EMDB-9714, PDB-6ira:
Structure of the human GluN1/GluN2A NMDA receptor in the glutamate/glycine-bound state at pH 7.8
Method: EM (single particle) / Resolution: 4.5 Å

9715

6irf

EMDB-9715, PDB-6irf:
Structure of the human GluN1/GluN2A NMDA receptor in the glutamate/glycine-bound state at pH 6.3, Class I
Method: EM (single particle) / Resolution: 5.1 Å

9716

6irg

EMDB-9716, PDB-6irg:
Structure of the human GluN1/GluN2A NMDA receptor in the glutamate/glycine-bound state at pH 6.3, Class II
Method: EM (single particle) / Resolution: 5.5 Å

9717

6irh

EMDB-9717, PDB-6irh:
Structure of the human GluN1/GluN2A NMDA receptor in the glutamate/glycine-bound state at pH 6.3, Class III
Method: EM (single particle) / Resolution: 7.8 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ionotropic glutamate receptors / NMDA receptors / synaptic protein

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