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Updated: Feb 16, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands
Alberto T Gatta1, Andrea C Sauerwein2, Anastasia Zhuravleva3
1UCL Institute of Ophthalmology, Department of Cell Biology, 11-43 Bath Street, London EC1V 9EL, UK.
Abstract:
Sterols are essential components of cellular membranes and shape their biophysical properties. The recently discovered family of Lipid transfer proteins Anchored at Membrane contact sites (LAMs) has been suggested to carry out intracellular sterol traffic using StART-like domains. Here, we studied the second StART-like domain of Lam4p from S. cerevisiae by NMR. We show that NMR data are consistent with the StART-like domain structure, and that several functionally important regions within the domain exhibit significant conformational dynamics. NMR titration experiments confirm sterol binding to the canonical sterol-binding site and suggest a role of membrane interactions on the thermodynamics and kinetics of sterol binding.
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