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Many cellular signalling and related events are triggered by the association of peripheral proteins with anionic lipids in the cell membrane (e.g. phosphatidylinositol phosphates or PIPs). This association frequently occurs via lipid-binding modules, e.g. pleckstrin homology (PH), C2 and four-point-one, ezrin, radixin, moesin (FERM) domains, present in peripheral and cytosolic proteins. Multiscale simulation approaches that combine coarse-grained and atomistic MD simulations may now be applied with confidence to investigate the molecular mechanisms of the association of peripheral proteins with model bilayers. Comparisons with experimental data indicate that such simulations can predict specific peripheral protein-lipid interactions. We discuss the application of multiscale MD simulation and related approaches to investigate the association of peripheral proteins which contain PH, C2 or FERM-binding modules with lipid bilayers of differing phospholipid composition, including bilayers containing multiple PIP molecules.

Original publication

DOI

10.1042/BST20140144

Type

Journal article

Journal

Biochem Soc Trans

Publication Date

10/2014

Volume

42

Pages

1418 - 1424

Keywords

Animals, Auxilins, Cattle, Ciona intestinalis, Humans, Lipid Bilayers, Models, Molecular, Molecular Dynamics Simulation, PTEN Phosphohydrolase, Phosphatidylinositol Phosphates, Phosphoric Monoester Hydrolases, Protein Structure, Tertiary, Protein Transport, Talin