Gatta, AT;
Sauerwein, AC;
Zhuravleva, A;
Levine, TP;
Matthews, S;
(2017)
Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands.
Biochemical and Biophysical Research Communications
, 495
(3)
pp. 2270-2274.
10.1016/j.bbrc.2017.12.109.
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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.
Type: | Article |
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Title: | Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands |
Location: | United States |
Open access status: | An open access version is available from UCL Discovery |
DOI: | 10.1016/j.bbrc.2017.12.109 |
Publisher version: | https://doi.org/10.1016/j.bbrc.2017.12.109 |
Language: | English |
Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions. |
Keywords: | Intracellular sterol traffic, Lipid transfer proteins, Membrane contact sites, Nuclear magnetic resonance, Protein-lipid interaction |
UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Ophthalmology |
URI: | https://discovery.ucl.ac.uk/id/eprint/10042287 |
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