Pannexin: Difference between revisions

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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/4'>lipid molecules</scene> which interact with hydrophobic sidechains<ref>PMID:35133866</ref>.  
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

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

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References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky