Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.

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...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awduron:	Antcliff, J, Haider, S, Proks, P, Sansom, MS, Ashcroft, F
Fformat:	Journal article
Iaith:	English
Cyhoeddwyd:	2005

Eitemau Tebyg

Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
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Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.
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Identification of residues contributing to the ATP binding site of Kir6.2.
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Direct photoaffinity labeling of the Kir6.2 subunit of the ATP-sensitive K+ channel by 8-azido-ATP.
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Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
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Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
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Glimepiride block of Kir6.2/SUR1 Kir6.2/SUR2A and Kir6.2/SUR2A and Kir6.2/SUR2B K-ATP channels.
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Time-dependent activation of Kir6.2/SUR2A channels but not Kir6.2/SUR1 channels in the presence of ATP
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Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.
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Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel.
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Time-dependent activation of KIR6.2/SUR2A channels but not KIR6.2/SUR1 channels in the presence of MgATP
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Photobiomodulation on KATP Channels of Kir6.2-Transfected HEK-293 Cells
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Reduced expression of Kir6.2/SUR2A subunits explains KATP deficiency in K+-depleted rats.
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Molecular determinants of KATP channel inhibition by ATP.
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Kir6.2-dependent high-affinity repaglinide binding to beta-cell K(ATP) channels.
gan: Hansen, A, et al.
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Molecular basis of Kir6.2 mutations causing neonatal diabetes and neonatal diabetes with neurological features
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A gating mutation at the internal mouth of the Kir6.2 pore is associated with DEND syndrome.
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Overlapping distribution of K(ATP) channel-forming Kir6.2 subunit and the sulfonylurea receptor SUR1 in rodent brain.
gan: Karschin, C, et al.
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Structure of an open KATP channel reveals tandem PIP2 binding sites mediating the Kir6.2 and SUR1 regulatory interface
gan: Camden M. Driggers, et al.
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The Kir6.2-F333I mutation differentially modulates K-ATP channels composed of SUR1 or SUR2 subunits
gan: Tammaro, P, et al.
Cyhoeddwyd: (2007)

The Kir6.2-F333I mutation differentially modulates K ATP channels composed of SUR1 and SUR2 subunits
gan: Tammaro, P, et al.
Cyhoeddwyd: (2007)

Direct photoaffinity labeling of Kir6.2 by [gamma-(32)P]ATP-[gamma]4-azidoanilide.
gan: Tanabe, K, et al.
Cyhoeddwyd: (2000)

Molecular basis of Kir6.2 mutations associated with neonatal diabetes or neonatal diabetes plus neurological features.
gan: Proks, P, et al.
Cyhoeddwyd: (2004)

Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor.
gan: Tucker, S, et al.
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A novel SUR1/Kir6.2 specific K-ATP channel opener
gan: Dabrowski, M, et al.
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