@article{oai:oist.repo.nii.ac.jp:00001793,
 author = {Lee, Hyuk-Joon and Jeong, Hyeongseop and Hyun, Jaekyung and Ryu, Bumhan and Park, Kunwoong and Lim, Hyun-Ho and Yoo, Jejoong and Woo, Jae-Sung},
 issue = {35},
 journal = {Science Advances},
 month = {Aug},
 note = {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-A 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 A and selectively transports chloride ions. Our study provides structural insights into the permeant selectivity of Cx31.3 hemichannel.},
 title = {Cryo-EM structure of human Cx31.3/GJC3 connexin hemichannel},
 volume = {6},
 year = {2020}
}