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Structure of human pannexin-1 with a blocked pore

ABSTRACT:

SUBMITTER: Atsunori Oshima

PROVIDER: EMPIAR-10758 | biostudies-other |

REPOSITORIES: biostudies-other

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Structures of human pannexin-1 in nanodiscs reveal gating mediated by dynamic movement of the N terminus and phospholipids.

Kuzuya Maki M Hirano Hidemi H Hayashida Kenichi K Watanabe Masakatsu M Kobayashi Kazumi K Terada Tohru T Mahmood Md Iqbal MI Tama Florence F Tani Kazutoshi K Fujiyoshi Yoshinori Y Oshima Atsunori A

Science signaling 20220208 720

Pannexin (PANX) family proteins form large-pore channels that mediate purinergic signaling. We analyzed the cryo-EM structures of human PANX1 in lipid nanodiscs to elucidate the gating mechanism and its regulation by the amino terminus in phospholipids. The wild-type channel has an amino-terminal funnel in the pore, but in the presence of the inhibitor probenecid, a cytoplasmically oriented amino terminus and phospholipids obstruct the pore. Functional analysis using whole-cell patch-clamp and o ...[more]

PMID: 35133866

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