2boc: Difference between revisions

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New page: left|200px<br /> <applet load="2boc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2boc, resolution 3.01Å" /> '''POTASSIUM CHANNEL K...
 
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[[Image:2boc.gif|left|200px]]<br />
[[Image:2boc.gif|left|200px]]<br /><applet load="2boc" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2boc" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2boc, resolution 3.01&Aring;" />
caption="2boc, resolution 3.01&Aring;" />
'''POTASSIUM CHANNEL KCSA-FAB COMPLEX IN THALLIUM WITH TETRAETHYLARSONIUM (TEAS)'''<br />
'''POTASSIUM CHANNEL KCSA-FAB COMPLEX IN THALLIUM WITH TETRAETHYLARSONIUM (TEAS)'''<br />


==Overview==
==Overview==
Potassium channels catalyze the selective transfer of potassium across the, cell membrane and are essential for setting the resting potential in, cells, controlling heart rate and modulating the firing pattern in, neurons. Tetraethylammonium (TEA) blocks ion conduction through potassium, channels in a voltage-dependent manner from both sides of the membrane., Here we show the structural basis of TEA blockade by cocrystallizing the, prokaryotic potassium channel KcsA with two selective TEA analogs. TEA, binding at both sites alters ion occupancy in the selectivity filter;, these findings underlie the mutual destabilization and voltage-dependence, of TEA blockade. We propose that TEA blocks potassium channels by acting, as a potassium analog at the dehydration transition step during, permeation.
Potassium channels catalyze the selective transfer of potassium across the cell membrane and are essential for setting the resting potential in cells, controlling heart rate and modulating the firing pattern in neurons. Tetraethylammonium (TEA) blocks ion conduction through potassium channels in a voltage-dependent manner from both sides of the membrane. Here we show the structural basis of TEA blockade by cocrystallizing the prokaryotic potassium channel KcsA with two selective TEA analogs. TEA binding at both sites alters ion occupancy in the selectivity filter; these findings underlie the mutual destabilization and voltage-dependence of TEA blockade. We propose that TEA blocks potassium channels by acting as a potassium analog at the dehydration transition step during permeation.


==About this Structure==
==About this Structure==
2BOC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans] with CO, TL and T1A as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BOC OCA].  
2BOC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans] with <scene name='pdbligand=CO:'>CO</scene>, <scene name='pdbligand=TL:'>TL</scene> and <scene name='pdbligand=T1A:'>T1A</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOC OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Streptomyces lividans]]
[[Category: Streptomyces lividans]]
[[Category: Focia, P.J.]]
[[Category: Focia, P J.]]
[[Category: Gross, A.]]
[[Category: Gross, A.]]
[[Category: Lenaeus, M.J.]]
[[Category: Lenaeus, M J.]]
[[Category: Vamvouka, M.]]
[[Category: Vamvouka, M.]]
[[Category: CO]]
[[Category: CO]]
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[[Category: protein-antibody fab complex]]
[[Category: protein-antibody fab complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:48:02 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:51 2008''

Revision as of 17:39, 21 February 2008

File:2boc.gif


2boc, resolution 3.01Å

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POTASSIUM CHANNEL KCSA-FAB COMPLEX IN THALLIUM WITH TETRAETHYLARSONIUM (TEAS)

OverviewOverview

Potassium channels catalyze the selective transfer of potassium across the cell membrane and are essential for setting the resting potential in cells, controlling heart rate and modulating the firing pattern in neurons. Tetraethylammonium (TEA) blocks ion conduction through potassium channels in a voltage-dependent manner from both sides of the membrane. Here we show the structural basis of TEA blockade by cocrystallizing the prokaryotic potassium channel KcsA with two selective TEA analogs. TEA binding at both sites alters ion occupancy in the selectivity filter; these findings underlie the mutual destabilization and voltage-dependence of TEA blockade. We propose that TEA blocks potassium channels by acting as a potassium analog at the dehydration transition step during permeation.

About this StructureAbout this Structure

2BOC is a Protein complex structure of sequences from Mus musculus and Streptomyces lividans with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of TEA blockade in a model potassium channel., Lenaeus MJ, Vamvouka M, Focia PJ, Gross A, Nat Struct Mol Biol. 2005 May;12(5):454-9. Epub 2005 Apr 24. PMID:15852022

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