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 specific tryptophan in the I-II linker is a key determinant of beta-subunit binding and modulation in Ca(V)2.3 calcium channels.

Biophysical journal - 1 Sept 2002

Berrou L, Klein H, Bernatchez G, Parent L

Abstract excerpt

The ancillary beta subunits modulate the activation and inactivation properties of high-voltage activated (HVA) Ca(2+) channels in an isoform-specific manner. The beta subunits bind to a high-affinity interaction site, alpha-interaction domain (AID), located in the I-II linker of HVA alpha1 subunits. Nine residues in the AID motif are absolutely conserved in all HVA channels (QQxExxLxGYxxWIxxxE), but their...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Calcium Channels
Share to Cation Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Electrophysiology

Share to Glutathione Transferase

Share to Tryptophan

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 12202369
DOI: 10.1016/S0006-3495(02)73914-3
PMCID: PMC1302242

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

A specific tryptophan in the I-II linker is a key determinant of beta-subunit binding and modulation in Ca(V)2.3 calcium channels.PMID 12202369Read ↗

The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.Semantic proximity Read ↗

The role of a voltage-dependent Ca2+ channel intracellular linker: a structure-function analysis.Semantic proximity Read ↗

Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation.Semantic proximity Read ↗

Ca(V)1.2 I-II linker structure and Timothy syndrome.Semantic proximity Read ↗

Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker.Semantic proximity Read ↗

A Polybasic Plasma Membrane Binding Motif in the I-II Linker Stabilizes Voltage-gated CaV1.2 Calcium Channel Function.Semantic proximity Read ↗

Identification of a surface charged residue in the S3-S4 linker of the pacemaker (HCN) channel that influences activation gating.Semantic proximity Read ↗

An interaction between the III-IV linker and CTD in NaV1.5 confers regulation of inactivation by CaM and FHF.Semantic proximity Read ↗

Hydrophobic interactions between the HA helix and S4-S5 linker modulate apparent Ca2+ sensitivity of SK2 channels.Semantic proximity Read ↗

Identification of a disulfide bridge essential for structure and function of the voltage-gated Ca(2+) channel α(2)δ-1 auxiliary subunit.Semantic proximity Read ↗

Investigating the Functional Role of the DI-DII Linker in Nav1.5 Channel FunctionSemantic proximity Read ↗

A conserved gating element in TRPV6 channels.Semantic proximity Read ↗

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