2dwd
From Proteopedia
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==Overview== | ==Overview== | ||
| - | K(+) channels play essential roles in regulating membrane excitability of | + | K(+) channels play essential roles in regulating membrane excitability of many diverse cell types by selectively conducting K(+) ions through their pores. Many diverse molecules can plug the pore and modulate the K(+) current. Quaternary ammonium (QA) ions are a class of pore blockers that have been used for decades by biophysicists to probe the pore, leading to important insights into the structure-function relation of K(+) channels. However, many key aspects of the QA-blocking mechanisms remain unclear to date, and understanding these questions requires high resolution structural information. Here, we address the question of whether intracellular QA blockade causes conformational changes of the K(+) channel selectivity filter. We have solved the structures of the KcsA K(+) channel in complex with tetrabutylammonium (TBA) and tetrabutylantimony (TBSb) under various ionic conditions. Our results demonstrate that binding of TBA or TBSb causes no significant change in the KcsA structure at high concentrations of permeant ions. We did observe the expected conformational change of the filter at low concentration of K(+), but this change appears to be independent of TBA or TBSb blockade. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystallographic | + | Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel., Yohannan S, Hu Y, Zhou Y, J Mol Biol. 2007 Feb 23;366(3):806-14. Epub 2006 Dec 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17196615 17196615] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tetrabutylammonium]] | [[Category: tetrabutylammonium]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:03:24 2008'' |
Revision as of 15:03, 21 February 2008
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crystal structure of KcsA-FAB-TBA complex in Tl+
Overview
K(+) channels play essential roles in regulating membrane excitability of many diverse cell types by selectively conducting K(+) ions through their pores. Many diverse molecules can plug the pore and modulate the K(+) current. Quaternary ammonium (QA) ions are a class of pore blockers that have been used for decades by biophysicists to probe the pore, leading to important insights into the structure-function relation of K(+) channels. However, many key aspects of the QA-blocking mechanisms remain unclear to date, and understanding these questions requires high resolution structural information. Here, we address the question of whether intracellular QA blockade causes conformational changes of the K(+) channel selectivity filter. We have solved the structures of the KcsA K(+) channel in complex with tetrabutylammonium (TBA) and tetrabutylantimony (TBSb) under various ionic conditions. Our results demonstrate that binding of TBA or TBSb causes no significant change in the KcsA structure at high concentrations of permeant ions. We did observe the expected conformational change of the filter at low concentration of K(+), but this change appears to be independent of TBA or TBSb blockade.
About this Structure
2DWD is a Single protein structure of sequence from Mus musculus and Streptomyces lividans with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel., Yohannan S, Hu Y, Zhou Y, J Mol Biol. 2007 Feb 23;366(3):806-14. Epub 2006 Dec 2. PMID:17196615
Page seeded by OCA on Thu Feb 21 17:03:24 2008
Categories: Mus musculus | Single protein | Streptomyces lividans | Yohannan, S. | Zhou, Y. | F09 | L2C | TBA | TL | K+ | Kcsa | Membrane protein | Potassium channel | Tetrabutylammonium
