@article{TEXTUAL,
      recid = {11525},
      author = {Hussain, Nazia and Apotikar, Ashish and Pidathala,  Shabareesh and Mukherjee, Sourajit and Burada, Ananth  Prasad and Sikdar, Sujit Kumar and Vinothkumar, Kutti R.  and Penmatsa, Aravind},
      title = {Cryo-EM structures of pannexin 1 and 3 reveal differences  among pannexin isoforms},
      journal = {Nature Communications},
      address = {2024-04-05},
      number = {TEXTUAL},
      abstract = {Pannexins are single-membrane large-pore channels that  release ions and ATP upon activation. Three isoforms of  pannexins 1, 2, and 3, perform diverse cellular roles and  differ in their pore lining residues. In this study, we  report the cryo-EM structure of pannexin 3 at 3.9 Å and  analyze its structural differences with pannexin isoforms 1  and 2. The pannexin 3 vestibule has two distinct chambers  and a wider pore radius in comparison to pannexins 1 and 2.  We further report two cryo-EM structures of pannexin 1,  with pore substitutions W74R/R75D that mimic the pore  lining residues of pannexin 2 and a germline mutant of  pannexin 1, R217H at resolutions of 3.2 Å and 3.9 Å,  respectively. Substitution of cationic residues in the  vestibule of pannexin 1 results in reduced ATP interaction  propensities to the channel. The germline mutant R217H in  transmembrane helix 3 (TM3), leads to a partially  constricted pore, reduced ATP interaction and weakened  voltage sensitivity. The study compares the three pannexin  isoform structures, the effects of substitutions of pore  and vestibule-lining residues and allosteric effects of a  pathological substitution on channel structure and function  thereby enhancing our understanding of this vital group of  ATP-release channels.},
      url = {http://knowledge.uchicago.edu/record/11525},
}