4pe5 | pdb_00004pe5

Crystal Structure of GluN1a/GluN2B NMDA Receptor Ion Channel

spinqualitylabelsall models 4pe5, resolution 3.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pe5 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, GLU, GLY, NAG, QEL, W, MAN Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Crystal structure of a heterotetrameric NMDA receptor ion channel.,Karakas E, Furukawa H Science. 2014 May 30;344(6187):992-7. doi: 10.1126/science.1251915. PMID:24876489 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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