Probing structural states of pentameric ligand-gated ion channels in match-out deuterated detergent
Pentameric ligand-gated ion channels mediate electrochemical signal transduction in neuronal and other cellular systems, and are critical targets of disease mutations and drugs. However, the structural changes associated with gating and modulation in this family remain unclear. The bacterial protein GLIC has provided a valuable model system, but has raised recent questions as to the functional states of known crystal structures, particularly the existence of an additional, more expanded open state. We propose to answer these questions by small-angle neutron scattering experiments, taking advantage of deuterated match-out detergents, and the high-flux and state-of-the-art detector at D22 to collect structural data free from crystal artefacts or detergent signal. Resolving between conflicting models of GLIC open and closed states in this way will provide critical templates for biophysical characterization and drug design.
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LYCKSELL Marie; ARLETH Lise; Rebecca J Howard; Nicolai Tidemand Johansen; LINDAHL Erik; MARTEL Anne; PORCAR Lionel and F.G. Tidemand. (2020). Probing structural states of pentameric ligand-gated ion channels in match-out deuterated detergent. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-987
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