date: 2020-09-01T10:59:52Z pdf:unmappedUnicodeCharsPerPage: 0 pdf:PDFVersion: 1.4 pdf:docinfo:title: The structure of a potassium-selective ion channel reveals a hydrophobic gate regulating ion permeation xmp:CreatorTool: pdftk 1.44 - www.pdftk.com dc:description: Protein dynamics are essential to function. One example of this is the various gating mechanisms within ion channels, which are transmembrane proteins that act as gateways into the cell. Typical ion channels switch between an open and closed state via a conformational transition which is often triggered by an external stimulus, such as ligand binding or pH and voltage differences. The atomic resolution structure of a potassium-selective ion channel named NaK2K has allowed us to observe that a hydro­phobic residue at the bottom of the selectivity filter, Phe92, appears in dual conformations. One of the two conformations of Phe92 restricts the diameter of the exit pore around the selectivity filter, limiting ion flow through the channel, while the other conformation of Phe92 provides a larger-diameter exit pore from the selectivity filter. Thus, it can be concluded that Phe92 acts as a hydro­phobic gate, regulating the flow of ions through the selectivity filter. access_permission:modify_annotations: true access_permission:can_print_degraded: true description: Protein dynamics are essential to function. One example of this is the various gating mechanisms within ion channels, which are transmembrane proteins that act as gateways into the cell. Typical ion channels switch between an open and closed state via a conformational transition which is often triggered by an external stimulus, such as ligand binding or pH and voltage differences. The atomic resolution structure of a potassium-selective ion channel named NaK2K has allowed us to observe that a hydro­phobic residue at the bottom of the selectivity filter, Phe92, appears in dual conformations. One of the two conformations of Phe92 restricts the diameter of the exit pore around the selectivity filter, limiting ion flow through the channel, while the other conformation of Phe92 provides a larger-diameter exit pore from the selectivity filter. Thus, it can be concluded that Phe92 acts as a hydro­phobic gate, regulating the flow of ions through the selectivity filter. dcterms:created: 2020-07-25T12:00:00Z Last-Modified: 2020-09-01T10:59:52Z dcterms:modified: 2020-09-01T10:59:52Z dc:format: application/pdf; version=1.4 title: The structure of a potassium-selective ion channel reveals a hydrophobic gate regulating ion permeation Last-Save-Date: 2020-09-01T10:59:52Z pdf:docinfo:creator_tool: pdftk 1.44 - www.pdftk.com access_permission:fill_in_form: true pdf:docinfo:modified: 2020-09-01T10:59:52Z meta:save-date: 2020-09-01T10:59:52Z pdf:encrypted: false dc:title: The structure of a potassium-selective ion channel reveals a hydrophobic gate regulating ion permeation modified: 2020-09-01T10:59:52Z Content-Type: application/pdf X-Parsed-By: org.apache.tika.parser.DefaultParser meta:creation-date: 2020-07-25T12:00:00Z created: 2020-07-25T12:00:00Z access_permission:extract_for_accessibility: true access_permission:assemble_document: true xmpTPg:NPages: 9 Creation-Date: 2020-07-25T12:00:00Z pdf:charsPerPage: 3161 access_permission:extract_content: true access_permission:can_print: true producer: International Union of Crystallography access_permission:can_modify: true pdf:docinfo:producer: International Union of Crystallography pdf:docinfo:created: 2020-07-25T12:00:00Z