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

Cryo-EM structure of the zinc-activated channel (ZAC) in the Cys-loop receptor superfamily.

Proceedings of the National Academy of Sciences of the United States of America - 29 Oct 2024

Jin Fei, Lin Yi-Yu, Wang Ru-Chun, Xie Tang-Xuan, Zhao Yimeng, Shen Cheng, Sheng Danqi, Ichikawa Muneyoshi, Yu Ye, Wang Jin, Hattori Motoyuki

Abstract excerpt

Cys-loop receptors are a large superfamily of pentameric ligand-gated ion channels with various physiological roles, especially in neurotransmission in the central nervous system. Among them, zinc-activated channel (ZAC) is a Zn2+-activated ion channel that is widely expressed in the human body and is conserved among eukaryotes. Due to its gating by extracellular Zn2+, ZAC has been considered a Zn2+ sensor, but...

Read the complete abstract on PubMed

Topics

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

Share to Cryoelectron Microscopy
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 39441630
DOI: 10.1073/pnas.2405659121
PMCID: PMC11536092

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

Cryo-EM structure of the zinc-activated channel (ZAC) in the Cys-loop receptor superfamily.PMID 39441630Read ↗

To be or not to be an ion channel: cryo-EM structures have a saySemantic proximity Read ↗

Structure of the receptor-activated human TRPC6 ion channelSemantic proximity Read ↗

Cryo-EM structure of the cytoplasmic domain of murine transient receptor potential cation channel subfamily C member 6 (TRPC6).Semantic proximity Read ↗

Probing the molecular basis for signal transduction through the Zinc-Activated Channel (ZAC).Semantic proximity Read ↗

Delineation of the functional properties exhibited by the Zinc-Activated Channel (ZAC) and its high-frequency Thr128Ala variant (rs2257020) in Xenopus oocytes.Semantic proximity Read ↗

A comprehensive search for calcium binding sites critical for TMEM16A calcium-activated chloride channel activity.Semantic proximity Read ↗

Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms.Semantic proximity Read ↗

Structural basis for pharmacological modulation of the TRPC6 channel.Semantic proximity Read ↗

Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complexSemantic proximity Read ↗

The two-domain elevator-type mechanism of zinc-transporting ZIP proteinsSemantic proximity Read ↗

Structural insights of ZIP4 extracellular domain critical for optimal zinc transport.Semantic proximity Read ↗

Structure of the human ClC-1 chloride channelSemantic proximity Read ↗

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