4PE5
Crystal Structure of GluN1a/GluN2B NMDA Receptor Ion Channel
Summary for 4PE5
| Entry DOI | 10.2210/pdb4pe5/pdb |
| Descriptor | Glutamate receptor ionotropic, NMDA 1, 4-[(1R,2S)-2-(4-benzylpiperidin-1-yl)-1-hydroxypropyl]phenol, GLUTAMIC ACID, ... (11 entities in total) |
| Functional Keywords | nmda receptor, glun1, glun2b, ion channel, transport protein |
| Biological source | Rattus norvegicus (Rat) More |
| Total number of polymer chains | 4 |
| Total formula weight | 392812.47 |
| Authors | Karakas, E.,Furukawa, H. (deposition date: 2014-04-22, release date: 2014-06-04, Last modification date: 2024-11-06) |
| Primary citation | Karakas, E.,Furukawa, H. Crystal structure of a heterotetrameric NMDA receptor ion channel. Science, 344:992-997, 2014 Cited by PubMed Abstract: N-Methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors, which mediate most excitatory synaptic transmission in mammalian brains. Calcium permeation triggered by activation of NMDA receptors is the pivotal event for initiation of neuronal plasticity. Here, we show the crystal structure of the intact heterotetrameric GluN1-GluN2B NMDA receptor ion channel at 4 angstroms. The NMDA receptors are arranged as a dimer of GluN1-GluN2B heterodimers with the twofold symmetry axis running through the entire molecule composed of an amino terminal domain (ATD), a ligand-binding domain (LBD), and a transmembrane domain (TMD). The ATD and LBD are much more highly packed in the NMDA receptors than non-NMDA receptors, which may explain why ATD regulates ion channel activity in NMDA receptors but not in non-NMDA receptors. PubMed: 24876489DOI: 10.1126/science.1251915 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.96 Å) |
Structure validation
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