NDLI: Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation

Content Provider	PubMed Central
Author	Sauer, David B. Zeng, Weizhong Raghunathan, Srinivasan Jiang, Youxing
Abstract	The structural and functional conversion of the nonselective NaK channel to a K+ selective channel (NaK2K) allows us to identify two key residues, Tyr and Asp in the filter sequence of TVGYGD, that participate in interactions central to stabilizing the K+ channel selectivity filter. By using protein crystallography and channel electrophysiology, we demonstrate that the K+ channel filter exists as an energetically strained structure and requires these key protein interactions working in concert to hold the filter in the precisely defined four-sited configuration that is essential for selective K+ permeation. Disruption of either interaction, as tested on both the NaK2K and eukaryotic K v 1.6 channels, can reduce or completely abolish K+ selectivity and in some cases may also lead to channel inactivation due to conformational changes at the filter. Additionally, on the scaffold of NaK we recapitulate the protein interactions found in the filter of the Kir channel family, which uses a distinct interaction network to achieve similar stabilization of the filter.
Related Links	http://dx.doi.org/10.1073/pnas.1111688108
Ending Page	16639
Page Count	6
Starting Page	16634
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	40
Volume Number	108
Language	English
Publisher	National Academy of Sciences
Publisher Date	2011-10-04
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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