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

Authors
Lee, Hyuk-JoonJeong, HyeongseopHyun, JaekyungRyu, BumhanPark, KunwoongLim, Hyun-HoYoo, JejoongWoo, Jae-Sung
Issue Date
8월-2020
Publisher
AMER ASSOC ADVANCEMENT SCIENCE
Citation
SCIENCE ADVANCES, v.6, no.35
Indexed
SCIE
SCOPUS
Journal Title
SCIENCE ADVANCES
Volume
6
Number
35
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/54320
DOI
10.1126/sciadv.aba4996
ISSN
2375-2548
Abstract
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-angstrom 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 similar to 8 angstrom and selectively transports chloride ions. Our study provides structural insights into the permeant selectivity of Cx31.3 hemichannel.
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