1qdv

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(New page: 200px<br /><applet load="1qdv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qdv, resolution 1.6&Aring;" /> '''N-TERMINAL DOMAIN, VO...)
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[[Image:1qdv.jpg|left|200px]]<br /><applet load="1qdv" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qdv.jpg|left|200px]]<br /><applet load="1qdv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qdv, resolution 1.6&Aring;" />
caption="1qdv, resolution 1.6&Aring;" />
'''N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131'''<br />
'''N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131'''<br />
==Overview==
==Overview==
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Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in, channel gating. However, structural alterations of these mutants leave, open the question concerning direct involvement of T1 in gating. We find, in mammalian Kv1.2 that gating depends critically on residues at, complementary T1 surfaces in an unusually polar interface. An isosteric, mutation in this interface causes surprisingly little structural, alteration while stabilizing the closed channel and increasing the, stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil, destabilizes the closed channel. Together, these data suggest that, structural changes involving the buried polar T1 surfaces play a key role, in the conformational changes leading to channel opening.
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Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening.
==About this Structure==
==About this Structure==
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1QDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QDV OCA].
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1QDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDV OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Berger, J.M.]]
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[[Category: Berger, J M.]]
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[[Category: Jan, L.Y.]]
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[[Category: Jan, L Y.]]
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[[Category: Jan, Y.N.]]
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[[Category: Jan, Y N.]]
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[[Category: Jr., D.L.Minor.]]
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[[Category: Jr., D L.Minor.]]
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[[Category: Lin, Y.F.]]
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[[Category: Lin, Y F.]]
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[[Category: Mobley, B.C.]]
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[[Category: Mobley, B C.]]
[[Category: Yu, M.]]
[[Category: Yu, M.]]
[[Category: intracellular gate]]
[[Category: intracellular gate]]
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[[Category: voltage-gated potassium channel]]
[[Category: voltage-gated potassium channel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:36:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:40 2008''

Revision as of 12:38, 21 February 2008


1qdv, resolution 1.6Å

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N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131

Overview

Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening.

About this Structure

1QDV is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel., Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM, Cell. 2000 Sep 1;102(5):657-70. PMID:11007484

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