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Absence of ion-binding affinity in the putatively inactivated low-[K+] structure of the KcsA potassium channel
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 749235
Author(s) Boiteux, Céline; Bernèche, Simon
Author(s) at UniBasel Bernèche, Simon
Year 2011
Title Absence of ion-binding affinity in the putatively inactivated low-[K+] structure of the KcsA potassium channel
Journal Structure
Volume 19
Number 1
Pages / Article-Number 70-9
Abstract Potassium channels are membrane proteins that selectively conduct K(+) across cellular membranes. The narrowest part of their pore, the selectivity filter, is responsible for distinguishing K(+) from Na(+), and can also act as a gate through a mechanism known as C-type inactivation. It has been proposed that a conformation of the KcsA channel obtained by crystallization in presence of low concentration of K(+) (PDB 1K4D) could correspond to the C-type inactivated state. Here, we show using molecular mechanics simulations that such conformation has little ion-binding affinity and that ions do not contribute to its stability. The simulations suggest that, in this conformation, the selectivity filter is mostly occupied by water molecules. Whether such ion-free state of the KcsA channel is physiologically accessible and representative of the inactivated state of eukaryotic channels remains unclear.
Publisher Current Biology
ISSN/ISBN 0969-2126
edoc-URL http://edoc.unibas.ch/dok/A5844205
Full Text on edoc No
Digital Object Identifier DOI 10.1016/j.str.2010.10.008
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/21220117
ISI-Number WOS:000286348000010
Document type (ISI) Journal Article
 
   

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