Ontology highlight
ABSTRACT:
SUBMITTER: Song X
PROVIDER: S-EPMC5962351 | biostudies-literature | 2018 Apr
REPOSITORIES: biostudies-literature
Song Xianqiang X Jensen Morten Ø MØ Jogini Vishwanath V Stein Richard A RA Lee Chia-Hsueh CH Mchaourab Hassane S HS Shaw David E DE Gouaux Eric E
Nature 20180418 7702
The NMDA (N-methyl-D-aspartate) receptor transduces the binding of glutamate and glycine, coupling it to the opening of a calcium-permeable ion channel <sup>1</sup> . Owing to the lack of high-resolution structural studies of the NMDA receptor, the mechanism by which ion-channel blockers occlude ion permeation is not well understood. Here we show that removal of the amino-terminal domains from the GluN1-GluN2B NMDA receptor yields a functional receptor and crystals with good diffraction properti ...[more]