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TitleCryo-EM structure of the human Pannexin-3 channel.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 745, Page 151227, Year 2025
Publish dateDec 20, 2024
AuthorsTaiichi Tsuyama / Ryuga Teramura / Kaoru Mitsuoka / Jun-Ichi Kishikawa / Ken Yokoyama /
PubMed AbstractPannexin-3 (PANX3) is a member of the pannexin family of large-pore, ATP-permeable channels conserved across vertebrates. PANX3 contributes to various developmental and pathophysiological processes ...Pannexin-3 (PANX3) is a member of the pannexin family of large-pore, ATP-permeable channels conserved across vertebrates. PANX3 contributes to various developmental and pathophysiological processes by permeating ATP and Ca ions; however, the structural basis of PANX3 channel function remains unclear. Here, we present the cryo-EM structure of human PANX3 at 2.9-3.2 Å. The PANX3 channel is heptameric and forms a transmembrane pore along the central symmetric axis. The narrowest constriction of the pore is composed of an isoleucine ring located in the extracellular region, and its size is comparable to that of other pannexins. A structural variability analysis revealed prominent structural dynamics in intracellular regions. Our structural studies provide a foundation for understanding the detailed properties of pannexin channels.
External linksBiochem Biophys Res Commun / PubMed:39721314
MethodsEM (single particle)
Resolution2.9 - 3.2 Å
Structure data

62478

9kom

EMDB-62478, PDB-9kom:
Cryo-EM structure of human pannexin-3 protomer
Method: EM (single particle) / Resolution: 3.2 Å

62526

9krg

EMDB-62526, PDB-9krg:
Cryo-EM structure of human pannexin-3 heptamer
Method: EM (single particle) / Resolution: 2.9 Å

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Pannexin / Innexin

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