한빛사논문
- 조회1,192
Hyuk-Joon Lee1,*, Hyeongseop Jeong1,2,*, Jaekyung Hyun2,3,*, Bumhan Ryu1, Kunwoong Park4, Hyun-Ho Lim4, Jejoong Yoo5,6 and Jae-Sung Woo1,†
1Department of Life Sciences, Korea University, Seoul 02841, Republic of Korea.
2Korea Basic Science Institute, Chungcheongbuk-do 28119, Republic of Korea.
3Molecular Cryo-electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa 904-0496, Japan.
4Neurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 41062 Daegu, Republic of Korea.
5Department of Physics, Sungkyunkwan University, Suwon, Republic of Korea.
6Center for Self-assembly and Complexity (CSC), Institute for Basic Science (IBS), Pohang 37673, Republic of Korea.
†Corresponding author.
*These authors contributed equally to this work.
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-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.
논문정보
- Research article
- 2020년 08월 (BRIC 등록일 2020-12-07)
- 국내(교신)+국외 연구진
- 생명과학 > 구조생물 및 생물물리학
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