[논문]Cryo-EM structure of human Cx31.3/GJC3 connexin hemichannel

Lee, Hyuk-Joon; Jeong, Hyeongseop; Hyun, Jaekyung; Ryu, Bumhan; Park, Kunwoong; Lim, Hyun-Ho; Yoo, Jejoong; Woo, Jae-Sung

doi:10.1126/sciadv.aba4996

[해외논문] Cryo-EM structure of human Cx31.3/GJC3 connexin hemichannel 원문보기

Science advances, v.6 no.35, 2020년, pp.eaba4996 -

Lee, Hyuk-Joon (Department of Life Sciences, Korea University, Seoul 02841, Republic of Korea.) , Jeong, Hyeongseop (Department of Life Sciences, Korea University, Seoul 02841, Republic of Korea.) , Hyun, Jaekyung (Korea Basic Science Institute, Chungcheongbuk-do 28119, Republic of Korea.) , Ryu, Bumhan (Department of Life Sciences, Korea University, Seoul 02841, Republic of Korea.) , Park, Kunwoong (Neurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 41062 Daegu, Republic of Korea.) , Lim, Hyun-Ho (Neurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 41062 Daegu, Republic of Korea.) , Yoo, Jejoong (Department of Physics, Sungkyunkwan University, Suwon, Republic of Korea.) , Woo, Jae-Sung (Department of Life Sciences, Korea University, Seoul 02841, Republic of Korea.)

Abstract ▼ AI-Helper

Cryo-EM structure of human connexin 31.3 hemichannel reveals the selective permeability mechanism.Connexin family proteins assemble into hexameric channels called hemichannels/connexons, which function as transmembrane channels or dock together to form gap junction intercellular channels (GJIChs). We determined the cryo–electron microscopy structures of human connexin 31.3 (Cx31.3)/GJC3 hemichannels in the presence and absence of calcium ions and with a hearing-loss mutation R15G at 2.3-, 2.5-, and 2.6-Å resolutions, respectively. Compared with available structures of GJICh in open conformation, Cx31.3 hemichannel shows substantial structural changes of highly conserved regions in the connexin family, including opening of calcium ion–binding tunnels, reorganization of salt-bridge networks, exposure of lipid-binding sites, and collocation of amino-terminal helices at the cytoplasmic entrance. We also found that the hemichannel has a pore with a diameter of ~8 Å and selectively transports chloride ions. Our study provides structural insights into the permeant selectivity of Cx31.3 hemichannel.

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