Size exclusion chromatography coupled SANS to elucidate the solution structure of three prokaryotic ligand-gated ion channels
Pentameric ligand-gated ion channels mediate fast signal transduction in a variety of excitable cells, and are important drug targets. These channels are also found in bacteria, where their function and dynamics remain largely unexplored. The prokaryotic channels are valuable model systems and may offer insights into states that are difficult to capture in the eukaryotic homologs, especially the conducting state. Structures of bacterial channels in this family have been solved with pore sizes ranging from wide to narrow, but uncertainty remain in the field as to how these states correspond to functional states. We propose to probe this question by using SANS to explore the variability in pore dimensions among the related bacterial channels ELIC, sTeLIC and DeCLIC. Use of deuterated detergent and the SEC-SANS capabilities of D22 will give structural data free from crystal artefacts and detergent signal. This investigation promises to demonstrate the value of SANS in annotating functional states of membrane proteins under room-temperature solution conditions, and to provide insights about the ion pores of the wide but poorly characterized family of bacterial ligand-gated channels.
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LYCKSELL Marie; ARLETH Lise; Rebecca J Howard; Nicolai Tidemand Johansen; LINDAHL Erik; MARTEL Anne; PORCAR Lionel and ROVSNIK Urska. (2020). Size exclusion chromatography coupled SANS to elucidate the solution structure of three prokaryotic ligand-gated ion channels. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1002
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