Albert Lau

Albert Lau

Associate Professor

Receptor ligand-interactions.
WBSB 706

Research Interests

Our lab uses a combination of computational and experimental approaches to try to understand the atomic and molecular details governing the function of protein complexes involved in intercellular communication. The complexes that are studied include ionotropic glutamate receptors (iGluRs). iGluRs are ligand-gated ion channels that mediate the majority of excitatory synaptic transmission in the central nervous system. iGluRs are important in synaptic plasticity, which underlies learning and memory. Receptor dysfunction has been implicated in a number of neurological disorders. The binding of neurotransmitter molecules to the ligand-binding domains of iGluRs drives the opening of the associated transmembrane pore, allowing cations to flow intothe cell, which in turn triggers a nerve impulse.   Albert Lau surface picture

Computationally, we apply methods in molecular simulation and statistical thermodynamics to estimate the free energies and kinetics associated with ligand binding and protein conformational transitions. Our goal is to generate testable predictions that can help guide experimental investigations as well as help interpret experimental observations. Computational protein design is also explored. Experimentally, we pursue structural studies primarily using X-ray crystallography to help characterize macromolecular structure-function relationships. Biophysical insights can collectively be applied to the design of theapeutic agents.

Complete List of Publications

Selected Publications

Wied TJ, Chin AC, and Lau AY. High conformational variability in the GluK2 kainate receptor ligand-binding domain. Structure, in press, 2018.

Yu A and Lau AY. Glutamate and glycine binding to the NMDA receptor. Structure 26, 1035–1043, 2018.

Yu A, Salazar H, Plested AJR, and Lau AY. Neurotransmitter funneling optimizes glutamate receptor kinetics. Neuron 97, 139–149, 2018.

Yu A and Lau AY. Energetics of glutamate binding to an ionotropic glutamate receptor. J Phys Chem B 121, 10436–10422, 2017.

Yu A, Alberstein R, Thomas A, Zimmet A, Grey R, Mayer ML, and Lau AY. Molecular lock regulates binding of glycine to a primitive NMDA receptor. Proc Natl Acad Sci USA 113, E6786–6795, 2016.