Protein Structure and Ion Binding in Potassium Selective Channels
type: CreativeWork
description: Potassium channels play a central role in a number of biological processes, most classically the action potential of excitable cells in multicellular organisms. These channels are defined by their selective conduction of potassium to the exclusion of other monovalent ions as governed by a common sequence and structural motif, the selectivity filter. This structure, made of backbone carbonyls and threonine side chains, directly coordinates the ions as they diffuse through the channel and appears central to this sub-angstrom discrimination between cations. Utilizing the non-selective Sodium and Potassium conducting channel (NaK) as a structural scaffold the mechanisms of both ion selectivity and formation of this selective structure are examined.
abstract: Potassium channels play a central role in a number of biological processes, most classically the action potential of excitable cells in multicellular organisms. These channels are defined by their selective conduction of potassium to the exclusion of other monovalent ions as governed by a common sequence and structural motif, the selectivity filter. This structure, made of backbone carbonyls and threonine side chains, directly coordinates the ions as they diffuse through the channel and appears central to this sub-angstrom discrimination between cations. Utilizing the non-selective Sodium and Potassium conducting channel (NaK) as a structural scaffold the mechanisms of both ion selectivity and formation of this selective structure are examined.
author: Sauer, David Bryant
keywords: Sodium-Potassium-Exchanging ATPase, Potassium, Models, Molecular
date published: 2013-01-17T16:18:48Z
date modified: 2026-07-24T05:52:06Z
provider: University of Texas Southwestern Medical Center
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Texas Southwestern Medical Center

PropertyValue
property ID: Handle
value: https://hdl.handle.net/2152.5/1262