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Open data
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Basic information
Entry | Database: PDB / ID: 7qey | |||||||||
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Title | human Connexin 26 class 1 hexamer at 90mmHg PCO2, pH7.4 | |||||||||
![]() | Gap junction beta-2 protein | |||||||||
![]() | MEMBRANE PROTEIN / Gap junction / Ion Channel / carbon dioxide sensitive | |||||||||
Function / homology | PHOSPHATIDYLETHANOLAMINE![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2 Å | |||||||||
![]() | Brotherton, D.H. / Cameron, A.D. / Savva, C.G. / Ragan, T.J. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Conformational changes and CO-induced channel gating in connexin26. Authors: Deborah H Brotherton / Christos G Savva / Timothy J Ragan / Nicholas Dale / Alexander D Cameron / ![]() Abstract: 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. ...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 (PCO) 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 PCO. We show a correlation between the level of PCO and the size of the aperture of the pore, governed by the N-terminal helices that line the pore. This indicates that CO 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. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 216.6 KB | Display | ![]() |
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PDB format | ![]() | 174 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 804.2 KB | Display | ![]() |
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Full document | ![]() | 812.8 KB | Display | |
Data in XML | ![]() | 35.7 KB | Display | |
Data in CIF | ![]() | 48.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 13944MC ![]() 7qeoC ![]() 7qeqC ![]() 7qerC ![]() 7qesC ![]() 7qetC ![]() 7qeuC ![]() 7qevC ![]() 7qewC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Assembly
Deposited unit | ![]()
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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