7qev: Difference between revisions
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
==human Connexin 26 at 55mm Hg PCO2, pH7.4:two masked subunits, class D== | |||
<StructureSection load='7qev' size='340' side='right'caption='[[7qev]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7qev]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QEV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7qev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qev OCA], [https://pdbe.org/7qev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qev RCSB], [https://www.ebi.ac.uk/pdbsum/7qev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qev ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Connexins form large-pore channels that function either as dodecameric gap junctions or hexameric hemichannels to allow the regulated movement of small molecules and ions across cell membranes. Opening or closing of the channels is controlled by a variety of stimuli, and dysregulation leads to multiple diseases. An increase in the partial pressure of carbon dioxide (PCO2) has been shown to cause connexin26 (Cx26) gap junctions to close. Here, we use cryoelectron microscopy (cryo-EM) to determine the structure of human Cx26 gap junctions under increasing levels of PCO2. We show a correlation between the level of PCO2 and the size of the aperture of the pore, governed by the N-terminal helices that line the pore. This indicates that CO2 alone is sufficient to cause conformational changes in the protein. Analysis of the conformational states shows that movements at the N terminus are linked to both subunit rotation and flexing of the transmembrane helices. | |||
Conformational changes and CO2-induced channel gating in connexin26.,Brotherton DH, Savva CG, Ragan TJ, Dale N, Cameron AD Structure. 2022 Mar 3. pii: S0969-2126(22)00046-6. doi:, 10.1016/j.str.2022.02.010. PMID:35276081<ref>PMID:35276081</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7qev" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Apurinic/apyrimidinic endonuclease 3D structures|Apurinic/apyrimidinic endonuclease 3D structures]] | |||
*[[Connexin 3D structure|Connexin 3D structure]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Brotherton DH]] | |||
[[Category: Cameron AD]] | |||
[[Category: Ragan TJ]] | |||
[[Category: Savva CG]] | |||
Latest revision as of 12:33, 9 October 2024
human Connexin 26 at 55mm Hg PCO2, pH7.4:two masked subunits, class Dhuman Connexin 26 at 55mm Hg PCO2, pH7.4:two masked subunits, class D
Structural highlights
Publication Abstract from PubMedConnexins form large-pore channels that function either as dodecameric gap junctions or hexameric hemichannels to allow the regulated movement of small molecules and ions across cell membranes. Opening or closing of the channels is controlled by a variety of stimuli, and dysregulation leads to multiple diseases. An increase in the partial pressure of carbon dioxide (PCO2) has been shown to cause connexin26 (Cx26) gap junctions to close. Here, we use cryoelectron microscopy (cryo-EM) to determine the structure of human Cx26 gap junctions under increasing levels of PCO2. We show a correlation between the level of PCO2 and the size of the aperture of the pore, governed by the N-terminal helices that line the pore. This indicates that CO2 alone is sufficient to cause conformational changes in the protein. Analysis of the conformational states shows that movements at the N terminus are linked to both subunit rotation and flexing of the transmembrane helices. Conformational changes and CO2-induced channel gating in connexin26.,Brotherton DH, Savva CG, Ragan TJ, Dale N, Cameron AD Structure. 2022 Mar 3. pii: S0969-2126(22)00046-6. doi:, 10.1016/j.str.2022.02.010. PMID:35276081[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||