Crystal structure of the potassium channel KirBac1.1 in the closed state.

Crystal structure of the potassium channel KirBac1.1 in the closed state.

The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in ga...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς:	Kuo, A, Gulbis, J, Antcliff, J, Rahman, T, Lowe, E, Zimmer, J, Cuthbertson, J, Ashcroft, F, Ezaki, T, Doyle, D
Μορφή:	Journal article
Γλώσσα:	English
Έκδοση:	2003

Παρόμοια τεκμήρια

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Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
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Permeation and gating in KirBac: Molecular dynamics simulations
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Filter flexibility and distortion in a bacterial inward rectifier K+ channel: simulation studies of KirBac1.1.
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Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating.
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Identification of gain of function mutations in KirBac potassium channels by genetic complementation in K+ auxotrophic strains of E-coli and yeast.
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ανά: Paynter, J, κ.ά.
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Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.
ανά: Paynter, J, κ.ά.
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ανά: Grottesi, A, κ.ά.
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The ligand-sensitive gate of a potassium channel lies close to the selectivity filter
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The ligand-sensitive gate of a potassium channel lies close to the selectivity filter.
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The ligand-sensitive gate of a potassium channel lies close to the selectivity filter
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Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1.
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Identification of mutations in Kir5.1 which affect time-dependent activation of heteromeric Kir4.1/Kir5.1 potassium channels
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Effects of mitiglinide (S 21403) on Kir6.2/SUR1, Kir6.2/SUR2A and Kir6.2/SUR2B types of ATP-sensitive potassium channel.
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Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
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Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels.
ανά: Shang, L, κ.ά.
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Structure-function studies of the fast gating kinetics of the cloned ATP-sensitive potassium channel, Kir6.2/SUR1
ανά: Proks, P, κ.ά.
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Identification of a heteromeric interaction that influences the rectification, gating, and pH sensitivity of Kir4.1/Kir5.1 potassium channels.
ανά: Casamassima, M, κ.ά.
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Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.
ανά: Antcliff, J, κ.ά.
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Molecular basis of Kir6.2 mutations causing neonatal diabetes and neonatal diabetes with neurological features
ανά: Proks, P, κ.ά.
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An in-frame deletion in Kir6.2 (KCNJ11) causing neonatal diabetes reveals a site of interaction between Kir6.2 and SUR1.
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Molecular dynamics simulations of inwardly rectifying (Kir) potassium channels: a comparative study.
ανά: Haider, S, κ.ά.
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Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes.
ανά: Gloyn, A, κ.ά.
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Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
ανά: Tucker, S, κ.ά.
Έκδοση: (1999)

Molecular basis of Kir6.2 mutations associated with neonatal diabetes or neonatal diabetes plus neurological features.
ανά: Proks, P, κ.ά.
Έκδοση: (2004)

No association of KIR3DL1 or KIR3DS1 or their alleles with ankylosing spondylitis.
ανά: McCappin, J, κ.ά.
Έκδοση: (2010)

Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.
ανά: Tammaro, P, κ.ά.
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INWARDLY RECTIFYING K+ CURRENTS IN OOCYTES CO-EXPRESSING KIR3.1 AND KIR3.2
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Multiple sites of interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
ανά: Jones, P, κ.ά.
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Glimepiride block of Kir6.2/SUR1 Kir6.2/SUR2A and Kir6.2/SUR2A and Kir6.2/SUR2B K-ATP channels.
ανά: Ashcroft, F, κ.ά.
Έκδοση: (2001)