Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.
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 bisphos...
Egile Nagusiak: | Haider, S, Tarasov, A, Craig, T, Sansom, M, Ashcroft, F |
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Formatua: | Journal article |
Hizkuntza: | English |
Argitaratua: |
2007
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Antzeko izenburuak
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Identification of residues contributing to the ATP binding site of Kir6.2.
nork: Trapp, S, et al.
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PIP(2)-binding site in Kir channels: definition by multiscale biomolecular simulations.
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PIP2-binding site in Kir channels: definition by multiscale biomolecular simulations
nork: Stansfeld, P, et al.
Argitaratua: (2009) -
Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
nork: Dabrowski, M, et al.
Argitaratua: (2004) -
Mapping the architecture of the ATP-binding site of Kir6.2
nork: Dabrowski, M, et al.
Argitaratua: (2002)