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Figure 1. Heptameric structure of the pannexin 1 channel.Side view (left) of the pannexin 1 structure resolved by Michalski et al., and top views of the extracellular region (EC; top right), the transmembrane region (TM; middle right), and the intracellular region (IC; bottom right). The arrangement of seven subunits to form the channel is clearly visible in the structure. Each of the three regions shown in the top views contains a constriction site in the pore that runs through the center of the protein, and the amino acid residues involved in the constriction sites are represented as pink spheres. Protein data bank ID: 6VD7. CT: C-terminus (yellow); NT: N-terminus (red).
Chekeni,
Pannexin 1 channels mediate 'find-me' signal release and membrane permeability during apoptosis.
2010, Pubmed
Chekeni,
Pannexin 1 channels mediate 'find-me' signal release and membrane permeability during apoptosis.
2010,
Pubmed
Kasuya,
Cryo-EM structures of the human volume-regulated anion channel LRRC8.
2018,
Pubmed
Ma,
Pannexin 1 forms an anion-selective channel.
2012,
Pubmed
Michalski,
The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition.
2020,
Pubmed
,
Xenbase
Michalski,
The weak voltage dependence of pannexin 1 channels can be tuned by N-terminal modifications.
2018,
Pubmed
Michalski,
Carbenoxolone inhibits Pannexin1 channels through interactions in the first extracellular loop.
2016,
Pubmed
Oshima,
Atomic structure of the innexin-6 gap junction channel determined by cryo-EM.
2016,
Pubmed
Sandilos,
Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region.
2012,
Pubmed
Syrjanen,
Structure and assembly of calcium homeostasis modulator proteins.
2020,
Pubmed
