6l3v: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==The R15G mutant of human Cx31.3/GJC3 connexin hemichannel== | ==The R15G mutant of human Cx31.3/GJC3 connexin hemichannel== | ||
<StructureSection load='6l3v' size='340' side='right'caption='[[6l3v]]' scene=''> | <StructureSection load='6l3v' size='340' side='right'caption='[[6l3v]], [[Resolution|resolution]] 2.63Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L3V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L3V FirstGlance]. <br> | <table><tr><td colspan='2'>[[6l3v]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L3V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L3V FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l3v OCA], [http://pdbe.org/6l3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l3v RCSB], [http://www.ebi.ac.uk/pdbsum/6l3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l3v ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMN:LAURYL+MALTOSE+NEOPENTYL+GLYCOL'>LMN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GJC3, GJE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l3v OCA], [http://pdbe.org/6l3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l3v RCSB], [http://www.ebi.ac.uk/pdbsum/6l3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l3v ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CXG3_HUMAN CXG3_HUMAN]] One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:32923625</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6l3v" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hyun J]] | [[Category: Hyun, J]] | ||
[[Category: Jeong H]] | [[Category: Jeong, H]] | ||
[[Category: Lee | [[Category: Lee, H J]] | ||
[[Category: Ryu B]] | [[Category: Ryu, B]] | ||
[[Category: Woo | [[Category: Woo, J S]] | ||
[[Category: Atp release]] | |||
[[Category: Gap junction]] | |||
[[Category: Hemichannel]] | |||
[[Category: Hexamer]] | |||
[[Category: Membrane protein]] | |||
Revision as of 10:21, 30 September 2020
The R15G mutant of human Cx31.3/GJC3 connexin hemichannelThe R15G mutant of human Cx31.3/GJC3 connexin hemichannel
Structural highlights
Function[CXG3_HUMAN] One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Publication Abstract from PubMedConnexin 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. References
|
| ||||||||||||||||||