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Structure paper

TitleStructural basis of human zinc-activated channel (ZAC) signaling and modulation.
Journal, issue, pagesCell Discov, Vol. 12, Issue 1, Year 2026
Publish dateMar 31, 2026
AuthorsZixuan Zhou / Yonghui Long / Yulin Chao / Chuanhui Yang / Yi-Quan Tang / Yilai Shu / Hongtao Zhu / Anders A Jensen / Qianhui Qu /
PubMed AbstractZinc (Zn) plays essential roles in a plethora of physiological processes, including key functions as a neuromodulator. The zinc-activated channel (ZAC) belongs to the Cys-loop receptor (CLR) ...Zinc (Zn) plays essential roles in a plethora of physiological processes, including key functions as a neuromodulator. The zinc-activated channel (ZAC) belongs to the Cys-loop receptor (CLR) superfamily of pentameric ligand-gated ion channels, which also comprises receptors for the important neurotransmitters acetylcholine, serotonin, GABA and glycine. In contrast to these classical CLRs, which have been extensively explored over decades, ZAC remains poorly characterized despite its potential significance in mammals. Here, we present several cryo-EM structures of human ZAC, including the ligand-free resting state, the Zn-bound state, and several antagonist-bound states. In the Zn-bound structure, Zn ions bind to the subunit interfaces of the extracellular domain, corresponding to the canonical agonist-binding sites in the classical CLRs, and are primarily coordinated through cation‒π interactions with two aromatic residues. While the antagonist TTFB inhibits ZAC by insertion between the transmembrane M2 helices of adjacent subunits, d-tubocurarine acts in a dual manner by blocking the channel and interfering with agonist binding. Combined with mutagenesis and electrophysiological analysis, these evaluations highlight the distinctive structural and functional features of this atypical CLR.
External linksCell Discov / PubMed:41912481 / PubMed Central
MethodsEM (single particle)
Resolution2.54 - 3.35 Å
Structure data

63033

9let

EMDB-63033, PDB-9let:
Cryo-EM structure of human ZAC in zinc Binding State
Method: EM (single particle) / Resolution: 2.62 Å

63034

9leu

EMDB-63034, PDB-9leu:
Cryo-EM structure of human ZAC with A152 mutant in zinc binding state
Method: EM (single particle) / Resolution: 2.63 Å

63035

9lev

EMDB-63035, PDB-9lev:
Cryo-EM structure of human ZAC in nanodisc in apo state
Method: EM (single particle) / Resolution: 3.35 Å

63036

9lex

EMDB-63036, PDB-9lex:
Cryo-EM structure of human ZAC in zinc partially binding state in nanodisc
Method: EM (single particle) / Resolution: 2.85 Å

63037

9ley

EMDB-63037, PDB-9ley:
Cryo-EM structure of human ZAC in complex with d-tubocurarine
Method: EM (single particle) / Resolution: 2.97 Å

63038

9lez

EMDB-63038, PDB-9lez:
Cryo-EM structure of human ZAC in complex with N-(4-(tert-butyl)thiazol-2-yl)-3-fluorobenzamide (TTFB)
Method: EM (single particle) / Resolution: 2.54 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-TC9:
D-TUBOCURARINE

PDB-1ekj:
THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM

Source
  • homo sapiens (human)
  • enterovirus a71
  • human enterovirus 71
KeywordsMEMBRANE PROTEIN / Cys-loop receptor / homopentamer / cation channel / zinc-binding state / d-tubocurarine-binding site / TTFB binding state

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