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-Structure paper
タイトル | Conformational changes and CO-induced channel gating in connexin26. |
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ジャーナル・号・ページ | Structure, Vol. 30, Issue 5, Page 697-706.e4, Year 2022 |
掲載日 | 2022年5月5日 |
著者 | Deborah H Brotherton / Christos G Savva / Timothy J Ragan / Nicholas Dale / Alexander D Cameron / |
PubMed 要旨 | 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. |
リンク | Structure / PubMed:35276081 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 1.9 - 2.9 Å |
構造データ | EMDB-13935, PDB-7qeo: EMDB-13937, PDB-7qeq: EMDB-13938, PDB-7qer: EMDB-13939, PDB-7qes: EMDB-13940, PDB-7qet: EMDB-13941, PDB-7qeu: EMDB-13942, PDB-7qev: EMDB-13943, PDB-7qew: EMDB-13944, PDB-7qey: |
化合物 | ChemComp-LMT: ChemComp-PTY: ChemComp-HOH: |
由来 |
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キーワード | MEMBRANE PROTEIN / Gap junction / Ion Channel / carbon dioxide sensitive |