Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.
ATP-sensitive potassium (KATP) channels couple cell metabolism to electrical activity by regulating K+ flux across the plasma membrane. Channel closure is mediated by ATP, which binds to the pore-forming subunit (Kir6.2). Here we use homology modelling and ligand docking to construct a model of the...
المؤلفون الرئيسيون: | Antcliff, J, Haider, S, Proks, P, Sansom, MS, Ashcroft, F |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2005
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مواد مشابهة
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Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
حسب: Dabrowski, M, وآخرون
منشور في: (2004) -
Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.
حسب: Haider, S, وآخرون
منشور في: (2005) -
Involvement of the N-terminus of Kir6.2 in the inhibition of the KATP channel by ATP.
حسب: Proks, P, وآخرون
منشور في: (1999) -
A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.
حسب: Tammaro, P, وآخرون
منشور في: (2007) -
Phentolamine block of KATP channels is mediated by Kir6.2.
حسب: Proks, P, وآخرون
منشور في: (1997)