Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.

Journal article

ATP-sensitive potassium (K(ATP)) channels couple cell metabolism to electrical activity by regulating K(+) fluxes across the plasma membrane. Channel closure is facilitated by ATP, which binds to the pore-forming subunit (Kir6.2). Conversely, channel opening is potentiated by phosphoinositol bisphosphate (PIP(2)), which binds to Kir6.2 and reduces channel inhibition by ATP. Here, we use homology modelling and ligand docking to identify the PIP(2)-binding site on Kir6.2. The model is consisten...

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Authors: Haider, S; Tarasov, A; Craig, T; Sansom, M; Ashcroft, F

• Publication status: Published
• Journal: EMBO journal
• Volume: 26
• Issue: 16
• Pages: 3749-3759
• Publication date: 2007-08-02
• DOI: 10.1038/sj.emboj.7601809
• EISSN: 1460-2075
• ISSN: 0261-4189
• Language: English
• Keywords: Animals; Molecular Sequence Data; Models, Molecular; Patch-Clamp Techniques; Protein Conformation; Humans; Rats; Mice; Potassium Channels, Inwardly Rectifying; Phosphatidylinositol 4,5-Diphosphate; Binding Sites; Adenosine Triphosphate; Protein Binding