7p5c

Cryo-EM structure of human TTYH3 in Ca2+ and GDN

spinqualitylabelsall models 7p5c, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7p5c is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Gene: TTYH3, KIAA1691 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TTYH3_HUMAN] Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction. Publication Abstract from PubMed 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(2+) 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. Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions.,Sukalskaia A, Straub MS, Deneka D, Sawicka M, Dutzler R Nat Commun. 2021 Aug 12;12(1):4893. doi: 10.1038/s41467-021-25106-4. PMID:34385445 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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