Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations

• Published in: Biochimica et biophysica acta Vol. 1858; no. 10; pp. 2390 - 2400
• Main Authors: Hedger, George, Sansom, Mark S.P.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-10-2016
• Subjects: Cardiolipin; Cholesterol; Lipid Bilayers - chemistry; Lipid binding site; Lipid–protein interaction; MD simulation; Membrane Proteins - chemistry; Membrane Transport Proteins - chemistry; Molecular Dynamics Simulation; PIP2; MD simulation; CG; ESR; EM; SERCA; Cholesterol; POPE; GABAAR; NMR; POPG; Kir; nAChR; MD; POPC; GPCR; Lipid–protein interaction; Cardiolipin; PIP2; ANT/AAC; β2AR; Lipid binding site; PIP
• ISSN: 0005-2736; 0006-3002; 1879-2642
• DOI: 10.1016/j.bbamem.2016.02.037

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 Róg.
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•Lipid molecules can selectively interact with specific sites on membrane proteins.•Lipid binding can modulate protein structure and function.•Molecular dynamics (MD) simulations provide a powerful tool for site identification.•MD has been used to identify sites on a wide range of membrane proteins.