Anionic phospholipid interactions with the potassium channel KcsA: simulation studies.

Journal article

Molecular dynamics (MD) simulations have been used to unmask details of specific interactions of anionic phospholipids with intersubunit binding sites on the surface of the bacterial potassium channel KcsA. Crystallographic data on a diacyl glycerol fragment at this site were used to model phosphatidylethanolamine (PE), or phosphatidylglycerol (PG), or phosphatidic acid (PA) at the intersubunit binding sites. Each of these models of a KcsA-lipid complex was embedded in phosphatidyl choline bi...

Expand abstract

Authors: Deol, S; Domene, C; Bond, P; Sansom, MS

• Publication status: Published
• Journal: Biophysical journal
• Volume: 90
• Issue: 3
• Pages: 822-830
• Publication date: 2006-02-01
• DOI: 10.1529/biophysj.105.071407
• EISSN: 1542-0086
• ISSN: 0006-3495
• Language: English
• Keywords: Phosphates; Pressure; Crystallography, X-Ray; Ions; Phosphatidylglycerols; Databases, Protein; Anions; Computer Simulation; Escherichia coli Proteins; Protein Folding; Temperature; Lipid Bilayers; Phospholipids; Lipids; Bacterial Proteins; Mutation; Models, Biological; Molecular Conformation; Potassium Channels; Models, Molecular; Binding Sites; Time Factors; Oxygen; Cell Membrane; Phosphatidylethanolamines; Phosphatidic Acids; Streptomyces lividans; Hydrogen Bonding; Potassium Channels, Voltage-Gated