1j95

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(New page: 200px<br /><applet load="1j95" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j95, resolution 2.8&Aring;" /> '''KCSA potassium channe...)
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[[Image:1j95.jpg|left|200px]]<br /><applet load="1j95" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j95.jpg|left|200px]]<br /><applet load="1j95" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1j95, resolution 2.8&Aring;" />
caption="1j95, resolution 2.8&Aring;" />
'''KCSA potassium channel with TBA (tetrabutylammonium) and potassium'''<br />
'''KCSA potassium channel with TBA (tetrabutylammonium) and potassium'''<br />
==Overview==
==Overview==
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Many voltage-dependent K+ channels open when the membrane is depolarized, and then rapidly close by a process called inactivation. Neurons use, inactivating K+ channels to modulate their firing frequency. In, Shaker-type K+ channels, the inactivation gate, which is responsible for, the closing of the channel, is formed by the channel's cytoplasmic amino, terminus. Here we show that the central cavity and inner pore of the K+, channel form the receptor site for both the inactivation gate and, small-molecule inhibitors. We propose that inactivation occurs by a, sequential reaction in which the gate binds initially to the cytoplasmic, channel surface and then enters the pore as an extended peptide. This, mechanism accounts for the functional properties of K+ channel, inactivation and indicates that the cavity may be the site of action for, certain drugs that alter cation channel function.
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Many voltage-dependent K+ channels open when the membrane is depolarized and then rapidly close by a process called inactivation. Neurons use inactivating K+ channels to modulate their firing frequency. In Shaker-type K+ channels, the inactivation gate, which is responsible for the closing of the channel, is formed by the channel's cytoplasmic amino terminus. Here we show that the central cavity and inner pore of the K+ channel form the receptor site for both the inactivation gate and small-molecule inhibitors. We propose that inactivation occurs by a sequential reaction in which the gate binds initially to the cytoplasmic channel surface and then enters the pore as an extended peptide. This mechanism accounts for the functional properties of K+ channel inactivation and indicates that the cavity may be the site of action for certain drugs that alter cation channel function.
==About this Structure==
==About this Structure==
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1J95 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans] with K and TBA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J95 OCA].
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1J95 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans] with <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=TBA:'>TBA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J95 OCA].
==Reference==
==Reference==
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[[Category: Streptomyces lividans]]
[[Category: Streptomyces lividans]]
[[Category: MacKinnon, R.]]
[[Category: MacKinnon, R.]]
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[[Category: Morais-Cabral, J.H.]]
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[[Category: Morais-Cabral, J H.]]
[[Category: Zhou, M.]]
[[Category: Zhou, M.]]
[[Category: K]]
[[Category: K]]
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[[Category: metal transport]]
[[Category: metal transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:01:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:00 2008''

Revision as of 11:20, 21 February 2008


1j95, resolution 2.8Å

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KCSA potassium channel with TBA (tetrabutylammonium) and potassium

Overview

Many voltage-dependent K+ channels open when the membrane is depolarized and then rapidly close by a process called inactivation. Neurons use inactivating K+ channels to modulate their firing frequency. In Shaker-type K+ channels, the inactivation gate, which is responsible for the closing of the channel, is formed by the channel's cytoplasmic amino terminus. Here we show that the central cavity and inner pore of the K+ channel form the receptor site for both the inactivation gate and small-molecule inhibitors. We propose that inactivation occurs by a sequential reaction in which the gate binds initially to the cytoplasmic channel surface and then enters the pore as an extended peptide. This mechanism accounts for the functional properties of K+ channel inactivation and indicates that the cavity may be the site of action for certain drugs that alter cation channel function.

About this Structure

1J95 is a Single protein structure of sequence from Streptomyces lividans with and as ligands. Full crystallographic information is available from OCA.

Reference

Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors., Zhou M, Morais-Cabral JH, Mann S, MacKinnon R, Nature. 2001 Jun 7;411(6838):657-61. PMID:11395760

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