Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.

The Journal of biological chemistry - 16 Jun 2017

Wang Shizhen, Borschel William F, Heyman Sarah, Hsu Phillip, Nichols Colin G

Abstract excerpt

The defining structural feature of inward-rectifier potassium (Kir) channels is the unique Kir cytoplasmic domain. Recently we showed that salt bridges located at the cytoplasmic domain subunit interfaces (CD-Is) of eukaryotic Kir channels control channel gating via stability of a novel inactivated closed state. The cytoplasmic domains of prokaryotic and eukaryotic Kir channels show similar conformational...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Burkholderia pseudomallei
Share to Lipid Bilayers

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Liposomes

Share to Phosphatidylinositol 4,5-Diphosphate

Share to Potassium Channels, Inwardly Rectifying

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to Structural Homology, Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 28446610
DOI: 10.1074/jbc.M117.785154
PMCID: PMC5473215

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.PMID 28446610Read ↗

KirBac1.1: it's an inward rectifying potassium channel.Semantic proximity Read ↗

Distant cytosolic residues mediate a two-way molecular switch that controls the modulation of inwardly rectifying potassium (Kir) channels by cholesterol and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)).Semantic proximity Read ↗

Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels.Semantic proximity Read ↗

Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.Semantic proximity Read ↗

Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies.Semantic proximity Read ↗

Structural rearrangements underlying ligand-gating in Kir channels.Semantic proximity Read ↗

Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1.Semantic proximity Read ↗

Identification of a heteromeric interaction that influences the rectification, gating, and pH sensitivity of Kir4.1/Kir5.1 potassium channels.Semantic proximity Read ↗

The Kir channel immunoglobulin domain is essential for Kir1.1 (ROMK) thermodynamic stability, trafficking and gating.Semantic proximity Read ↗

Extracellular Kir2.1C122Y Mutant Upsets Kir2.1-PIP2 Bonds and Is Arrhythmogenic in Andersen-Tawil Syndrome.Semantic proximity Read ↗

Three pairs of weak interactions precisely regulate the G-loop gate of Kir2.1 channel.Semantic proximity Read ↗

Biochemical, biophysical, and structural investigations of two mutants (C154Y and R312H) of the human Kir2.1 channel involved in the Andersen-Tawil syndrome.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.