Ontology highlight
ABSTRACT:
SUBMITTER: Durham RJ
PROVIDER: S-EPMC7035515 | biostudies-literature | 2020 Feb
REPOSITORIES: biostudies-literature
Durham Ryan J RJ Paudyal Nabina N Carrillo Elisa E Bhatia Nidhi Kaur NK Maclean David M DM Berka Vladimir V Dolino Drew M DM Gorfe Alemayehu A AA Jayaraman Vasanthi V
Proceedings of the National Academy of Sciences of the United States of America 20200203 7
Allostery can be manifested as a combination of repression and activation in multidomain proteins allowing for fine tuning of regulatory mechanisms. Here we have used single molecule fluorescence resonance energy transfer (smFRET) and molecular dynamics simulations to study the mechanism of allostery underlying negative cooperativity between the two agonists glutamate and glycine in the NMDA receptor. These data show that binding of one agonist leads to conformational flexibility and an increase ...[more]