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/ | 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>. | ||
==3D structures of pannexin== | ==3D structures of pannexin== | ||
[[Pannexin 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 07:46, 19 April 2026
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