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

Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.

Structure (London, England : 1993) - 1 Dec 2005

Fallon Jennifer L, Halling D Brent, Hamilton Susan L, Quiocho Florante A

Abstract excerpt

Ca2+-dependent inactivation (CDI) and facilitation (CDF) of the Ca(v)1.2 Ca2+ channel require calmodulin binding to a putative IQ motif in the carboxy-terminal tail of the pore-forming subunit. We present the 1.45 A crystal structure of Ca2+-calmodulin bound to a 21 residue peptide corresponding to the IQ domain of Ca(v)1.2. This structure shows that parallel binding of calmodulin to the IQ domain is governed by...

Read the complete abstract on PubMed

Topics

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

Share to Calcium Channels, L-Type
Share to Calmodulin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Mutation

Share to Peptides

Share to Protein Binding

Share to Protein Conformation

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 16338416
DOI: 10.1016/j.str.2005.09.021

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.PMID 16338416Read ↗

Apocalmodulin and Ca2+ calmodulin-binding sites on the CaV1.2 channel.Semantic proximity Read ↗

Half-calcified calmodulin promotes basal activity and inactivation of the L-type calcium channel CaV1.2.Semantic proximity Read ↗

Identification of the components controlling inactivation of voltage-gated Ca2+ channels.Semantic proximity Read ↗

α-Actinin-1 promotes activity of the L-type Ca2+ channel Cav 1.2.Semantic proximity Read ↗

Characterization of the calmodulin-binding site in the N terminus of CaV1.2.Semantic proximity Read ↗

An unconventional calmodulin-anchoring site within the AB module of Kv7.2 channels.Semantic proximity Read ↗

Voltage Gated Calcium Channel Dysregulation May Contribute to Neurological Symptoms in CalmodulinopathiesSemantic proximity Read ↗

Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+ binding and cause misfolding.Semantic proximity Read ↗

FRET two-hybrid mapping reveals function and location of L-type Ca2+ channel CaM preassociation.Semantic proximity Read ↗

NaV1.2 EFL domain allosterically enhances Ca2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD.Semantic proximity Read ↗

Arrhythmogenic calmodulin variants D131E and Q135P disrupt interaction with the L-type voltage-gated Ca2+ channel (Cav1.2) and reduce Ca2+-dependent inactivation.Semantic proximity Read ↗

A Mechanism of Calmodulin Modulation of the Human Cardiac Sodium Channel.Semantic proximity Read ↗

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