Pannexin
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The 3D structure of human <scene name='91/916893/Cv/3'>PNX1 shows the pore to constitute 7 subunits</scene>. The C-terminal of PNX1 is cleaved by caspase to produce an active PNX1. The pore transmembrane domains are occupied by <scene name='91/916893/Cv/ | + | The 3D structure of human <scene name='91/916893/Cv/3'>PNX1 shows the pore to constitute 7 subunits</scene>. The C-terminal of PNX1 is cleaved by caspase to produce an active PNX1. The pore transmembrane domains are occupied by <scene name='91/916893/Cv/5'>lipid molecules which interact predominantly with hydrophobic residues</scene><ref>PMID:35133866</ref>. |
Revision as of 14:47, 12 July 2022
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References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
