期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1858, 期 10, 页码 2390-2400出版社
ELSEVIER
DOI: 10.1016/j.bbamem.2016.02.037
关键词
Lipid-protein interaction; Lipid binding site; MD simulation; Cholesterol; Cardiolipin; PIP2
资金
- BBSRC [BB/L002558/1]
- Wellcome Trust [WT092970]
- MRC
- University of Oxford
- BBSRC [BB/L002558/1] Funding Source: UKRI
- EPSRC [EP/J010421/1, EP/L000253/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L002558/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J010421/1, EP/L000253/1] Funding Source: researchfish
- Medical Research Council [1514534] Funding Source: researchfish
Lipid molecules are able to selectively interact with specific sites on integral membrane proteins, and modulate their structure and function. Identification and characterization of these sites are of importance for our understanding of the molecular basis of membrane protein function and stability, and may facilitate the design of lipid-like drug molecules. Molecular dynamics simulations provide a powerful tool for the identification of these sites, complementing advances in membrane protein structural biology and biophysics. We describe recent notable biomolecular simulation studies which have identified lipid interaction sites on a range of different membrane proteins. The sites identified in these simulation studies agree well with those identified by complementary experimental techniques. This demonstrates the power of the molecular dynamics approach in the prediction and characterization of lipid interaction sites on integral membrane proteins. This article is part of a Special Issue entitled: Biosimulations edited by Ilpo Vattulainen and Tomasz Rog. (C) 2016 Published by Elsevier B.V.
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