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

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...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awduron:	Haider, S, Tarasov, A, Craig, T, Sansom, M, Ashcroft, F
Fformat:	Journal article
Iaith:	English
Cyhoeddwyd:	2007

Eitemau Tebyg

Identification of residues contributing to the ATP binding site of Kir6.2.
gan: Trapp, S, et al.
Cyhoeddwyd: (2003)

PIP(2)-binding site in Kir channels: definition by multiscale biomolecular simulations.
gan: Stansfeld, P, et al.
Cyhoeddwyd: (2009)

PIP2-binding site in Kir channels: definition by multiscale biomolecular simulations
gan: Stansfeld, P, et al.
Cyhoeddwyd: (2009)

Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
gan: Dabrowski, M, et al.
Cyhoeddwyd: (2004)

Mapping the architecture of the ATP-binding site of Kir6.2
gan: Dabrowski, M, et al.
Cyhoeddwyd: (2002)

Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.
gan: Antcliff, J, et al.
Cyhoeddwyd: (2005)

Investigating the PIP2 Binding Site in Kir Channels Via Multi-Scale Biomolecular Simulations
gan: Stansfeld, P, et al.
Cyhoeddwyd: (2010)

Glimepiride block of Kir6.2/SUR1 Kir6.2/SUR2A and Kir6.2/SUR2A and Kir6.2/SUR2B K-ATP channels.
gan: Ashcroft, F, et al.
Cyhoeddwyd: (2001)

Simulating PIP2-Induced Gating Transitions in Kir6.2 Channels
gan: Michael Bründl, et al.
Cyhoeddwyd: (2021-08-01)

An in-frame deletion in Kir6.2 (KCNJ11) causing neonatal diabetes reveals a site of interaction between Kir6.2 and SUR1.
gan: Craig, T, et al.
Cyhoeddwyd: (2009)

Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.
gan: Haider, S, et al.
Cyhoeddwyd: (2005)

Effects of mitiglinide (S 21403) on Kir6.2/SUR1, Kir6.2/SUR2A and Kir6.2/SUR2B types of ATP-sensitive potassium channel.
gan: Reimann, F, et al.
Cyhoeddwyd: (2001)

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.
Cyhoeddwyd: (2024-03-01)

Time-dependent activation of Kir6.2/SUR2A channels but not Kir6.2/SUR1 channels in the presence of ATP
gan: Ashcroft, F, et al.
Cyhoeddwyd: (2001)

Time-dependent activation of KIR6.2/SUR2A channels but not KIR6.2/SUR1 channels in the presence of MgATP
gan: Song, D, et al.
Cyhoeddwyd: (2001)

Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.
gan: Tammaro, P, et al.
Cyhoeddwyd: (2005)

A gating mutation at the internal mouth of the Kir6.2 pore is associated with DEND syndrome.
gan: Proks, P, et al.
Cyhoeddwyd: (2005)

A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.
gan: Tammaro, P, et al.
Cyhoeddwyd: (2007)

Phentolamine block of KATP channels is mediated by Kir6.2.
gan: Proks, P, et al.
Cyhoeddwyd: (1997)

Filter flexibility in a mammalian K channel: models and simulations of Kir6.2 mutants.
gan: Capener, C, et al.
Cyhoeddwyd: (2003)

Multiple sites of interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
gan: Jones, P, et al.
Cyhoeddwyd: (2001)

Permanent neonatal diabetes caused by an in-frame deletion in the N-terminus of Kir6.2
gan: Craig, T, et al.
Cyhoeddwyd: (2008)

Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
gan: Reimann, F, et al.
Cyhoeddwyd: (1999)

The N-terminus of Kir6.2 is involved in coupling to SUR1
gan: Reimann, F, et al.
Cyhoeddwyd: (1999)

Kir6.2-dependent high-affinity repaglinide binding to beta-cell K(ATP) channels.
gan: Hansen, A, et al.
Cyhoeddwyd: (2005)

Molecular basis of Kir6.2 mutations causing neonatal diabetes and neonatal diabetes with neurological features
gan: Proks, P, et al.
Cyhoeddwyd: (2005)

Involvement of the N-terminus of Kir6.2 in the inhibition of the KATP channel by ATP.
gan: Proks, P, et al.
Cyhoeddwyd: (1999)

3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1.
gan: Mikhailov, M, et al.
Cyhoeddwyd: (2005)

Interaction of the cytosolic domains of the Kir6.2 subunit of the K(ATP) channel is modulated by sulfonylureas.
gan: Lippiat, J, et al.
Cyhoeddwyd: (2002)

Screening for mutations in the Kir6.2 subunit of the beta-cell K-ATP channel
gan: Sakura, H, et al.
Cyhoeddwyd: (1996)

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

Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
gan: Tucker, S, et al.
Cyhoeddwyd: (1999)

Functional analysis of two Kir6.2 (KCNJ11) mutations, K170T and E322K, causing neonatal diabetes.
gan: Tarasov, A, et al.
Cyhoeddwyd: (2007)

Computer modelling and simulation studies of a human inwardly rectifying potassium channel Kir6.2
gan: Capener, C, et al.
Cyhoeddwyd: (2000)

Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor.
gan: Tucker, S, et al.
Cyhoeddwyd: (1997)

A novel SUR1/Kir6.2 specific K-ATP channel opener
gan: Dabrowski, M, et al.
Cyhoeddwyd: (2001)

Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
gan: Deacon, R, et al.
Cyhoeddwyd: (2006)

Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
gan: Deacon, R, et al.
Cyhoeddwyd: (2006)

Pyridine nucleotide regulation of the KATP channel Kir6.2/SUR1 expressed in Xenopus oocytes.
gan: Dabrowski, M, et al.
Cyhoeddwyd: (2003)

Functional analysis of six Kir6.2 (KCNJ11) mutations causing neonatal diabetes.
gan: Girard, C, et al.
Cyhoeddwyd: (2006)