Structural highlights
FunctionPANX3_HUMAN Regulator of osteoblast differentiation by functionning as a Ca(2+) channel in the endoplasmic reticulum which regulates calmodulin (CaM) pathways. Allows ATP release into the extracellular space and activation or purinergic receptors.[UniProtKB:Q8CEG0] Publication Abstract from PubMedPannexin-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(2+) 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 A. 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. Cryo-EM structure of the human Pannexin-3 channel.,Tsuyama T, Teramura R, Mitsuoka K, Kishikawa JI, Yokoyama K Biochem Biophys Res Commun. 2025 Jan;745:151227. doi: 10.1016/j.bbrc.2024.151227. , Epub 2024 Dec 20. PMID:39721314[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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