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

A universally conserved residue in the SUR1 subunit of the KATP channel is essential for translating nucleotide binding at SUR1 into channel opening.

The Journal of physiology - 15 Oct 2012

de Wet Heidi, Shimomura Kenju, Aittoniemi Jussi, Ahmad Nawaz, Lafond Mathilde, Sansom Mark S P, Ashcroft Frances M

Abstract excerpt

The sulphonylurea receptor (SUR1) subunit of the ATP-sensitive potassium (KATP) channel is a member of the ATP-binding cassette (ABC) protein family. Binding of MgADP to nucleotide-binding domain 2 (NBD2) is critical for channel activation.We identified a residue in NBD2 (G1401) that is fully conserved among ABC proteins and whose functional importance is unknown. Homology modelling places G1401 on the outer...

Read the complete abstract on PubMed

Topics

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

Share to Ion Channel Gating
Share to Maltose-Binding Proteins

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

Share to Nucleotides

Share to Oocytes

Share to Potassium Channels, Inwardly Rectifying

Share to Receptors, Drug

Share to Sulfonylurea Receptors

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 22802590
DOI: 10.1113/jphysiol.2012.236075
PMCID: PMC3495298

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

A universally conserved residue in the SUR1 subunit of the KATP channel is essential for translating nucleotide binding at SUR1 into channel opening.PMID 22802590Read ↗

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

A mutation (R826W) in nucleotide-binding domain 1 of ABCC8 reduces ATPase activity and causes transient neonatal diabetes.Semantic proximity Read ↗

Potassium channel regulation.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 ↗

Molecular determinants of KATP channel inhibition by ATP.Semantic proximity Read ↗

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

Mutation in nucleotide-binding domains of sulfonylurea receptor 2 evokes Na-ATP-dependent activation of ATP-sensitive K+ channels: implication for dimerization of nucleotide-binding domains to induce channel opening.Semantic proximity Read ↗

Substitution of the Walker A lysine by arginine in the nucleotide-binding domains of sulphonylurea receptor SUR2B: effects on ligand binding and channel activity.Semantic proximity Read ↗

Functional clustering of mutations in the dimer interface of the nucleotide binding folds of the sulfonylurea receptor.Semantic proximity Read ↗

Hyperinsulinism-Causing Mutations Cause Multiple Molecular Defects in SUR1 NBD1.Semantic proximity Read ↗

A functional role of the C-terminal 42 amino acids of SUR2A and SUR2B in the physiology and pharmacology of cardiovascular ATP-sensitive K(+) channels.Semantic proximity Read ↗

Potassium channel openers require ATP to bind to and act through sulfonylurea receptors.Semantic proximity Read ↗

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