9kom

Cryo-EM structure of human pannexin-3 protomer

spinqualitylabelsall models 9kom, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9kom is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PANX3_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 PubMed 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(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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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