Computer Simulations Predict High Structural Heterogeneity of Functional State of NMDA Receptors.

ABSTRACT: N-methyl-D-aspartate receptors (NMDARs)-i.e., transmembrane proteins expressed in neurons-play a central role in the molecular mechanisms of learning and memory formation. It is unclear how the known atomic structures of NMDARs determined by x-ray crystallography and electron cryomicroscopy (18 published Protein Data Bank entries) relate to the functional states of NMDARs inferred from electrophysiological recordings (multiple closed, open, preopen, etc. states). We address this problem by using molecular dynamics simulations at atomic resolution, a method successfully applied in the past to much smaller biomolecules. Our simulations predict that several conformations of NMDARs with experimentally determined geometries, including four "nonactive" electron cryomicroscopy structures, rapidly

SUBMITTER: Sinitskiy AV 

PROVIDER: S-EPMC6127453 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature