9KRG
Cryo-EM structure of human pannexin-3 heptamer
Summary for 9KRG
| Entry DOI | 10.2210/pdb9krg/pdb |
| Related | 9KOM |
| EMDB information | 62478 62526 |
| Descriptor | Pannexin-3 (1 entity in total) |
| Functional Keywords | pannexin, innexin, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 45965.45 |
| Authors | |
| Primary citation | Tsuyama, T.,Teramura, R.,Mitsuoka, K.,Kishikawa, J.I.,Yokoyama, K. Cryo-EM structure of the human Pannexin-3 channel. Biochem.Biophys.Res.Commun., 745:151227-151227, 2025 Cited by PubMed Abstract: 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. PubMed: 39721314DOI: 10.1016/j.bbrc.2024.151227 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
Download full validation report
