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

Regulation of K+ flow by a ring of negative charges in the outer pore of BKCa channels. Part I: Aspartate 292 modulates K+ conduction by external surface charge effect.

The Journal of general physiology - 1 Aug 2004

Haug Trude, Sigg Daniel, Ciani Sergio, Toro Ligia, Stefani Enrico, Olcese Riccardo

Abstract excerpt

The pore region of the majority of K+ channels contains the highly conserved GYGD sequence, known as the K+ channel signature sequence, where the GYG is critical for K+ selectivity (Heginbotham, L., T. Abramson, and R. MacKinnon. 1992. Science. 258:1152-1155). Exchanging the aspartate residue with asparagine in this sequence abolishes ionic conductance of the Shaker K+ channel (D447N) (Hurst, R.S., L. Toro, and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Aspartic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Large-Conductance Calcium-Activated Potassium Channel alpha Subunits

Share to Molecular Sequence Data

Share to Mutation

Share to Potassium

Share to Potassium Channels

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 15277578
DOI: 10.1085/jgp.200308949
PMCID: PMC2229624

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

Regulation of K+ flow by a ring of negative charges in the outer pore of BKCa channels. Part I: Aspartate 292 modulates K+ conduction by external surface charge effect.PMID 15277578Read ↗

Regulation of K+ flow by a ring of negative charges in the outer pore of BKCa channels. Part II: Neutralization of aspartate 292 reduces long channel openings and gating current slow component.Semantic proximity Read ↗

Role of hydrophobic and ionic forces in the movement of S4 of the Shaker potassium channel.Semantic proximity Read ↗

Intrinsic electrostatic potential in the BK channel pore: role in determining single channel conductance and block.Semantic proximity Read ↗

Regulation of large-conductance Ca <sup>2+</sup> - and voltage-gated K <sup>+</sup> channels by electrostatic interactions with auxiliary β subunitsSemantic proximity Read ↗

Mechanism of voltage sensing in Ca2+- and voltage-activated K+ (BK) channels.Semantic proximity Read ↗

Electrostatic interactions in the channel cavity as an important determinant of potassium channel selectivity.Semantic proximity Read ↗

Mechanism for attenuated outward conductance induced by mutations in the cytoplasmic pore of Kir2.1 channels.Semantic proximity Read ↗

BK channel opening involves side-chain reorientation of multiple deep-pore residues.Semantic proximity Read ↗

Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes.Semantic proximity Read ↗

Charges in the cytoplasmic pore control intrinsic inward rectification and single-channel properties in Kir1.1 and Kir2.1 channels.Semantic proximity Read ↗

Divalent cations slow activation of EAG family K+ channels through direct binding to S4.Semantic proximity Read ↗

Ion permeation through a voltage- sensitive gating pore in brain sodium channels having voltage sensor mutations.Semantic proximity Read ↗

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