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-Structure paper
タイトル | Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 4893, Year 2021 |
掲載日 | 2021年8月12日 |
著者 | Anastasiia Sukalskaia / Monique S Straub / Dawid Deneka / Marta Sawicka / Raimund Dutzler / |
PubMed 要旨 | The Tweety homologs (TTYHs) are members of a conserved family of eukaryotic membrane proteins that are abundant in the brain. The three human paralogs were assigned to function as anion channels that ...The Tweety homologs (TTYHs) are members of a conserved family of eukaryotic membrane proteins that are abundant in the brain. The three human paralogs were assigned to function as anion channels that are either activated by Ca or cell swelling. To uncover their unknown architecture and its relationship to function, we have determined the structures of human TTYH1-3 by cryo-electron microscopy. All structures display equivalent features of a dimeric membrane protein that contains five transmembrane segments and an extended extracellular domain. As none of the proteins shows attributes reminiscent of an anion channel, we revisited functional experiments and did not find any indication of ion conduction. Instead, we find density in an extended hydrophobic pocket contained in the extracellular domain that emerges from the lipid bilayer, which suggests a role of TTYH proteins in the interaction with lipid-like compounds residing in the membrane. |
リンク | Nat Commun / PubMed:34385445 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.2 - 4.0 Å |
構造データ | EMDB-13194, PDB-7p54: EMDB-13198, PDB-7p5c: EMDB-13200, PDB-7p5j: EMDB-13201, PDB-7p5m: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | LIPID TRANSPORT / Membrane protein / lipid metabolism |