Pannexin

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Current revision (08:05, 21 August 2023) (edit) (undo)
 
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[[6wbf]], [[6wbg]], [[6wbk]] – hPNX1 residues 1-373 – Cryo EM<br />
[[6wbf]], [[6wbg]], [[6wbk]] – hPNX1 residues 1-373 – Cryo EM<br />
[[6wbi]], [[6wbl]], [[6wbm]], [[6wbn]] – hPNX1 (mutant) residues 1-373 – Cryo EM<br />
[[6wbi]], [[6wbl]], [[6wbm]], [[6wbn]] – hPNX1 (mutant) residues 1-373 – Cryo EM<br />
 +
[[7xlb]], [[8f7c]] – hPNX2 - Cryo EM<br />
 +
[[7xl6]] – hPNX3 - Cryo EM<br />
 +
[[8a3b]] – mPNX1 – mouse - Cryo EM<br />
[[6uzy]], [[6vd7]] – PNX1 – western clawed frog – Cryo EM<br />
[[6uzy]], [[6vd7]] – PNX1 – western clawed frog – Cryo EM<br />
</StructureSection>
</StructureSection>

Current revision

Human pannexin 1 complex with lipid (PDB ID (7f8o)

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References

  1. Penuela S, Gehi R, Laird DW. The biochemistry and function of pannexin channels. Biochim Biophys Acta. 2013 Jan;1828(1):15-22. doi: 10.1016/j.bbamem.2012.01.017. , Epub 2012 Jan 28. PMID:22305965 doi:http://dx.doi.org/10.1016/j.bbamem.2012.01.017
  2. Sandilos JK, Chiu YH, Chekeni FB, Armstrong AJ, Walk SF, Ravichandran KS, Bayliss DA. Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region. J Biol Chem. 2012 Mar 30;287(14):11303-11. doi: 10.1074/jbc.M111.323378. Epub, 2012 Feb 6. PMID:22311983 doi:http://dx.doi.org/10.1074/jbc.M111.323378
  3. Penuela S, Harland L, Simek J, Laird DW. Pannexin channels and their links to human disease. Biochem J. 2014 Aug 1;461(3):371-81. doi: 10.1042/BJ20140447. PMID:25008946 doi:http://dx.doi.org/10.1042/BJ20140447
  4. Kuzuya M, Hirano H, Hayashida K, Watanabe M, Kobayashi K, Terada T, Mahmood MI, Tama F, Tani K, Fujiyoshi Y, Oshima A. Structures of human pannexin-1 in nanodiscs reveal gating mediated by dynamic movement of the N terminus and phospholipids. Sci Signal. 2022 Feb 8;15(720):eabg6941. doi: 10.1126/scisignal.abg6941. Epub, 2022 Feb 8. PMID:35133866 doi:http://dx.doi.org/10.1126/scisignal.abg6941

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