7sj1 | pdb_00007sj1

Structure of shaker-W434F

spinqualitylabelsall models 7sj1, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.9Å Ligands: K, POV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Voltage-activated potassium (Kv) channels open upon membrane depolarization and proceed to spontaneously inactivate. Inactivation controls neuronal firing rates and serves as a form of short-term memory and is implicated in various human neurological disorders. Here, we use high-resolution cryo-electron microscopy and computer simulations to determine one of the molecular mechanisms underlying this physiologically crucial process. Structures of the activated Shaker Kv channel and of its W434F mutant in lipid bilayers demonstrate that C-type inactivation entails the dilation of the ion selectivity filter and the repositioning of neighboring residues known to be functionally critical. Microsecond-scale molecular dynamics trajectories confirm that these changes inhibit rapid ion permeation through the channel. This long-sought breakthrough establishes how eukaryotic K(+) channels self-regulate their functional state through the plasticity of their selectivity filters. Structure of the Shaker Kv channel and mechanism of slow C-type inactivation.,Tan XF, Bae C, Stix R, Fernandez-Marino AI, Huffer K, Chang TH, Jiang J, Faraldo-Gomez JD, Swartz KJ Sci Adv. 2022 Mar 18;8(11):eabm7814. doi: 10.1126/sciadv.abm7814. Epub 2022 Mar, 18. PMID:35302848 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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