5wie: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/KCAB2_RAT KCAB2_RAT]] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. [[http://www.uniprot.org/uniprot/KCNA2_RAT KCNA2_RAT]] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.<ref>PMID:7544443</ref> | [[http://www.uniprot.org/uniprot/KCAB2_RAT KCAB2_RAT]] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. [[http://www.uniprot.org/uniprot/KCNA2_RAT KCNA2_RAT]] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.<ref>PMID:7544443</ref> | ||
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== Publication Abstract from PubMed == | |||
C-type inactivation underlies important roles played by voltage-gated K+ (Kv) channels. Functional studies have provided strong evidence that a common underlying cause of this type of inactivation is an alteration near the extracellular end of the channel's ion-selectivity filter. Unlike N-type inactivation, which is known to reflect occlusion of the channel's intracellular end, the structural mechanism of C-type inactivation remains controversial and may have many detailed variations. Here we report that in voltage-gated Shaker K+ channels lacking N-type inactivation, a mutation enhancing inactivation disrupts the outermost K+ site in the selectivity filter. Furthermore, in a crystal structure of the Kv1.2-2.1 chimeric channel bearing the same mutation, the outermost K+ site, which is formed by eight carbonyl-oxygen atoms, appears to be slightly too small to readily accommodate a K+ ion and in fact exhibits little ion density; this structural finding is consistent with the functional hallmark of C-type inactivation. | |||
Crystal structure of an inactivated mutant mammalian voltage-gated K+ channel.,Pau V, Zhou Y, Ramu Y, Xu Y, Lu Z Nat Struct Mol Biol. 2017 Aug 28. doi: 10.1038/nsmb.3457. PMID:28846092<ref>PMID:28846092</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
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