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

Kir6.2-D323 and SUR2A-Q1336: an intersubunit interaction pairing for allosteric information transfer in the KATP channel complex.

The Biochemical journal - 14 Feb 2020

Brennan Sean, Rubaiy Hussein N, Imanzadeh Saba, Reid Ruth, Lodwick David, Norman Robert I, Rainbow Richard D

Abstract excerpt

ATP-sensitive potassium (KATP) channels are widely expressed and play key roles in many tissues by coupling metabolic state to membrane excitability. The SUR subunits confer drug and enhanced nucleotide sensitivity to the pore-forming Kir6 subunit, and so information transfer between the subunits must occur. In our previous study, we identified an electrostatic interaction between Kir6 and SUR2 subunits that was...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Site
Share to ATP-Binding Cassette Transporters

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to KATP Channels

Share to Models, Structural

Share to Patch-Clamp Techniques

Share to Potassium Channels, Inwardly Rectifying

Share to Sulfonylurea Receptors

Source

Open in PubMed Open full text

Identifiers

PMID: 31957808
DOI: 10.1042/BCJ20190753
PMCID: PMC7015859

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kir6.2-D323 and SUR2A-Q1336: an intersubunit interaction pairing for allosteric information transfer in the KATP channel complex.PMID 31957808Read ↗

The Kir6.2-F333I mutation differentially modulates KATP channels composed of SUR1 or SUR2 subunits.Semantic proximity Read ↗

ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies.Semantic proximity Read ↗

Review. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator.Semantic proximity Read ↗

A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.Semantic proximity Read ↗

Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.Semantic proximity Read ↗

Personalized Therapeutics for KATP-Dependent Pathologies.Semantic proximity Read ↗

Engineered Kir6.2 mutations that correct the trafficking defect of K(ATP) channels caused by specific SUR1 mutations.Semantic proximity Read ↗

Three C-terminal residues from the sulphonylurea receptor contribute to the functional coupling between the K(ATP) channel subunits SUR2A and Kir6.2.Semantic proximity Read ↗

Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.Semantic proximity Read ↗

N-terminal transmembrane domain of SUR1 controls gating of Kir6.2 by modulating channel sensitivity to PIP2.Semantic proximity Read ↗

Functional analysis of six Kir6.2 (KCNJ11) mutations causing neonatal diabetes.Semantic proximity Read ↗

Mechanism of action of a sulphonylurea receptor SUR1 mutation (F132L) that causes DEND syndrome.Semantic proximity Read ↗

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