7YFF
Structure of GluN1a-GluN2D NMDA receptor in complex with agonist glycine and competitive antagonist CPP.
Summary for 7YFF
| Entry DOI | 10.2210/pdb7yff/pdb |
| EMDB information | 33788 |
| Descriptor | Glutamate receptor ionotropic, NMDA 1, Glutamate receptor ionotropic, NMDA 2D, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | ion channel, cryo-em structure, glutamate receptor, synaptic protein, electron transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 386627.11 |
| Authors | Zhang, J.L.,Zhu, S.J.,Zhang, M. (deposition date: 2022-07-08, release date: 2023-04-12, Last modification date: 2023-08-02) |
| Primary citation | Zhang, J.,Zhang, M.,Wang, Q.,Wen, H.,Liu, Z.,Wang, F.,Wang, Y.,Yao, F.,Song, N.,Kou, Z.,Li, Y.,Guo, F.,Zhu, S. Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits. Nat.Struct.Mol.Biol., 30:629-639, 2023 Cited by PubMed Abstract: N-methyl-D-aspartate (NMDA) receptors are heterotetramers comprising two GluN1 and two alternate GluN2 (N2A-N2D) subunits. Here we report full-length cryo-EM structures of the human N1-N2D di-heterotetramer (di-receptor), rat N1-N2C di-receptor and N1-N2A-N2C tri-heterotetramer (tri-receptor) at a best resolution of 3.0 Å. The bilobate N-terminal domain (NTD) in N2D intrinsically adopts a closed conformation, leading to a compact NTD tetramer in the N1-N2D receptor. Additionally, crosslinking the ligand-binding domain (LBD) of two N1 protomers significantly elevated the channel open probability (Po) in N1-N2D di-receptors. Surprisingly, the N1-N2C di-receptor adopted both symmetric (minor) and asymmetric (major) conformations, the latter further locked by an allosteric potentiator, PYD-106, binding to a pocket between the NTD and LBD in only one N2C protomer. Finally, the N2A and N2C subunits in the N1-N2A-N2C tri-receptor display a conformation close to one protomer in the N1-N2A and N1-N2C di-receptors, respectively. These findings provide a comprehensive structural understanding of diverse function in major NMDA receptor subtypes. PubMed: 36959261DOI: 10.1038/s41594-023-00959-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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