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

BK channel opening involves side-chain reorientation of multiple deep-pore residues.

Proceedings of the National Academy of Sciences of the United States of America - 7 Jan 2014

Chen Xixi, Yan Jiusheng, Aldrich Richard W

Abstract excerpt

Three deep-pore locations, L312, A313, and A316, were identified in a scanning mutagenesis study of the BK (Ca(2+)-activated, large-conductance K(+)) channel S6 pore, where single aspartate substitutions led to constitutively open mutant channels (L312D, A313D, and A316D). To understand the mechanisms of the constitutive openness of these mutant channels, we individually mutated these three sites into the other...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Electrophysiological Phenomena

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Ion Channel Gating

Share to Large-Conductance Calcium-Activated Potassium Channels

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 24367115
DOI: 10.1073/pnas.1321697111
PMCID: PMC3890798

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

BK channel opening involves side-chain reorientation of multiple deep-pore residues.PMID 24367115Read ↗

A residue at the cytoplasmic entrance of BK-type channels regulating single-channel opening by its hydrophobicity.Semantic proximity Read ↗

Contribution of the central hydrophobic residue in the PXP motif of voltage-dependent K+ channels to S6 flexibility and gating properties.Semantic proximity Read ↗

Structural basis of voltage-dependent gating in BK channels.Semantic proximity Read ↗

A role for the S0 transmembrane segment in voltage-dependent gating of BK channels.Semantic proximity Read ↗

Gating of shaker-type channels requires the flexibility of S6 caused by prolines.Semantic proximity Read ↗

An S6 mutation in BK channels reveals beta1 subunit effects on intrinsic and voltage-dependent gating.Semantic proximity Read ↗

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.Semantic proximity Read ↗

The conserved phenylalanine in the K+ channel voltage-sensor domain creates a barrier with unidirectional effects.Semantic proximity Read ↗

A side chain in S6 influences both open-state stability and ion permeation in a voltage-gated K+ channel.Semantic proximity Read ↗

Investigating the putative glycine hinge in Shaker potassium channel.Semantic proximity Read ↗

From Selective Permeation to Physiology in Potassium Channels.Semantic proximity Read ↗

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

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