Title : Crystal structure of a heterotetrameric
NMDA receptor ion
channel
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
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