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

Open-state structure and pore gating mechanism of the cardiac sodium channel.

Cell - 30 Sept 2021

Jiang Daohua, Banh Richard, Gamal El-Din Tamer M, Tonggu Lige, Lenaeus Michael J, Pomès Régis, Zheng Ning, Catterall William A

Abstract excerpt

The heartbeat is initiated by voltage-gated sodium channel NaV1.5, which opens rapidly and triggers the cardiac action potential; however, the structural basis for pore opening remains unknown. Here, we blocked fast inactivation with a mutation and captured the elusive open-state structure. The fast inactivation gate moves away from its receptor, allowing asymmetric opening of pore-lining S6 segments, which bend...

Read the complete abstract on PubMed

Topics

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

Share to Arrhythmias, Cardiac
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heart Rate

Share to Ion Channel Gating

Share to Myocardium

Share to NAV1.5 Voltage-Gated Sodium Channel

Share to Sodium

Source

Open in PubMed Open full text

Identifiers

PMID: 34520724
DOI: 10.1016/j.cell.2021.08.021
PMCID: PMC8673466

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Open-state structure and pore gating mechanism of the cardiac sodium channel.PMID 34520724Read ↗

When the Gates Swing Open Only: Arrhythmia Mutations That Target the Fast Inactivation Gate of Nav1.5.Semantic proximity Read ↗

Structure of human Na <sub>v</sub> 1.5 reveals the fast inactivation-related segments as a mutational hotspot for the Long QT SyndromeSemantic proximity Read ↗

Structural basis of human Nav1.5 gating mechanismsSemantic proximity Read ↗

Mapping Structural Distribution and Gating-Property Impacts of Disease-Associated Missense Mutations in Voltage-Gated Sodium ChannelsSemantic proximity Read ↗

Veratridine Can Bind to a Site at the Mouth of the Channel Pore at Human Cardiac Sodium Channel NaV1.5Semantic proximity Read ↗

Structure of human Nav1.5 reveals the fast inactivation-related segments as a mutational hotspot for the long QT syndrome.Semantic proximity Read ↗

Structural basis for pore blockade of the human cardiac sodium channel Na <sub>v</sub> 1.5 by tetrodotoxin and quinidineSemantic proximity Read ↗

A misstep in the multistep process of fast inactivation.Semantic proximity Read ↗

The cardiac sodium channel: gating function and molecular pharmacology.Semantic proximity Read ↗

Regulation and drug modulation of a voltage-gated sodium channel: Pivotal role of the S4-S5 linker in activation and slow inactivation.Semantic proximity Read ↗

E1784K, the most common Brugada syndrome and long-QT syndrome type 3 mutant, disrupts sodium channel inactivation through two separate mechanisms.Semantic proximity Read ↗

Multiple interactions between cytoplasmic domains regulate slow deactivation of Kv11.1 channels.Semantic proximity Read ↗

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