Gatta, AT, Sauerwein, AC, Zhuravleva, A et al. (2 more authors) (2018) 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. ISSN 0006-291X
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 2017, Elsevier Inc. All rights reserved. This is an author produced version of a paper published in Biochemical and Biophysical Research Communications. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Lipid transfer proteins Membrane contact sites Intracellular sterol traffic Protein-lipid interaction Nuclear magnetic resonance |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 01 Mar 2018 10:54 |
Last Modified: | 20 Dec 2018 01:39 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.bbrc.2017.12.109 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:127850 |