Stefan, Christopher;
Covino, Roberto;
(2024)
Making lipids very unhappy to discover how they bind to proteins.
Journal of Cell Biology
, 223
(11)
, Article e202410022. 10.1083/jcb.202410022.
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Abstract
Membrane lipid composition is maintained by conserved lipid transfer proteins, but computational approaches to study their lipid-binding mechanisms are limiting. Srinivasan et al. (https://doi.org/10.1083/jcb.202312055) develop a clever molecular dynamics simulations assay to accurately model lipid-binding poses in lipid transfer proteins.
Type: | Article |
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Title: | Making lipids very unhappy to discover how they bind to proteins |
Location: | United States |
Open access status: | An open access version is available from UCL Discovery |
DOI: | 10.1083/jcb.202410022 |
Publisher version: | http://dx.doi.org/10.1083/jcb.202410022 |
Language: | English |
Additional information: | © 2024 Stefan and Covino. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
Keywords: | Molecular Dynamics Simulation, Protein Binding, Carrier Proteins, Humans, Membrane Lipids, Lipids |
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 Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Lab for Molecular Cell Bio MRC-UCL |
URI: | https://discovery-pp.ucl.ac.uk/id/eprint/10198598 |
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