Parametrisation of the free energy of ATP binding to wild-type and mutant Kir6.2 potassium channels.

Journal article

ATP-sensitive K(+) (K(ATP)) channels, comprised of pore-forming Kir6.x and regulatory SURx subunits, play important roles in many cellular functions; because of their sensitivity to inhibition by intracellular ATP, K(ATP) channels provide a link between cell metabolism and membrane electrical activity. We constructed structural homology models of Kir6.2 and a series of Kir6.2 channels carrying mutations within the putative ATP-binding site. Computational docking was carried out to determine t...

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Authors: Moran, O; Grottesi, A; Chadburn, A; Tammaro, P

• Publication status: Published
• Journal: Biophysical chemistry
• Volume: 171
• Pages: 76-83
• Publication date: 2013-01-01
• DOI: 10.1016/j.bpc.2012.10.006
• EISSN: 1873-4200
• ISSN: 0301-4622
• Language: English
• Keywords: Animals; Molecular Sequence Data; Rats; Molecular Docking Simulation; Potassium Channels, Inwardly Rectifying; Structural Homology, Protein; Binding Sites; Thermodynamics; Adenosine Triphosphate; Mutation; Amino Acid Sequence; Sequence Alignment