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Biophysics and Biophysical Chemistry
725 N. Wolfe St
Baltimore, MD 21205
Molecular mechanics of allostery and binding
Research in my laboratory is focused on understanding the molecular mechanisms of multi-subunit assemblies involved in synaptic communication. We are particularly interested in elucidating the structural thermodynamics that govern subunit assembly, ligand binding, and allosteric control of neurotransmitter receptors. Our approach relies on a blend of computational and experimental methods in biophysics to define functionally important structural features and dynamics in macromolecular complexes. Many studies in my laboratory involve ionotropic glutamate receptors, which are large, tetrameric ion channel protein complexes that transduce chemical signals at synapses into electrical impulses. These studies have elucidated the molecular mechanics that control key aspects of ligand binding and protein conformational transitions that are critical to receptor function.
Wied TJ, Chin AC, Lau AY. High conformational variability in the GluK2 kainate receptor ligand-binding domain. Structure 27, 189–195, 2019. PMID: 30482727.
Yu A, Lau AY. Glutamate and glycine binding to the NMDA receptor. Structure 26, 1035–1043, 2018. PMID: 29887499.
Yu A, Salazar H, Plested AJR, Lau AY. Neurotransmitter funneling optimizes glutamate receptor kinetics. Neuron 97, 139–149, 2018. PMID: 29249286.
Yu A, Lau AY. Energetics of glutamate binding to an ionotropic glutamate receptor. J Phys Chem B 121, 10436–10442, 2017. PMID: 29065265.
Yu A, Alberstein R, Thomas A, Zimmet A, Grey R, Mayer ML, Lau AY. Molecular lock regulates binding of glycine to a primitive NMDA receptor. Proc. Natl. Acad. Sci. USA, 113, E6786–E6795, 2016. PMID: 27791085.