@article{7910c9349cda4838916bff58b9d82e34,
title = "Glutamate and Glycine Binding to the NMDA Receptor",
abstract = "In the N-methyl-D-aspartic acid receptor family of ionotropic glutamate receptors, the agonist glutamate and its co-agonist glycine bind to their respective subunits by different dynamic mechanisms. Glutamate binding is assisted by structural features on the receptor surface. Glycine binding does not receive such assistance.",
keywords = "NMDA receptors, free energy calculations, glutamate receptors, ligand binding, molecular dynamics simulations",
author = "Alvin Yu and Lau, {Albert Y.}",
note = "Funding Information: We thank Dominique Frueh for helpful discussion. Anton computer time was provided by the Pittsburgh Supercomputing Center (PSC) through NIH grant R01GM116961 . The Anton and Anton2 machines at PSC were generously made available by D.E. Shaw Research. This study also used resources provided by the Maryland Advanced Research Computing Center (MARCC) at Johns Hopkins University. This work was supported by NIH grant R01GM094495 (to A.Y.L.). Funding Information: We thank Dominique Frueh for helpful discussion. Anton computer time was provided by the Pittsburgh Supercomputing Center (PSC) through NIH grant R01GM116961. The Anton and Anton2 machines at PSC were generously made available by D.E. Shaw Research. This study also used resources provided by the Maryland Advanced Research Computing Center (MARCC) at Johns Hopkins University. This work was supported by NIH grant R01GM094495 (to A.Y.L.).",
year = "2018",
month = jul,
day = "3",
doi = "10.1016/j.str.2018.05.004",
language = "English (US)",
volume = "26",
pages = "1035--1043.e2",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "7",
}