6l3v

Publication Abstract from PubMed

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.

Cryo-EM structure of human Cx31.3/GJC3 connexin hemichannel.,Lee HJ, Jeong H, Hyun J, Ryu B, Park K, Lim HH, Yoo J, Woo JS Sci Adv. 2020 Aug 28;6(35):eaba4996. doi: 10.1126/sciadv.aba4996. eCollection, 2020 Aug. PMID:32923625^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.