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1t1d

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(New page: 200px<br /><applet load="1t1d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1d, resolution 1.51&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1t1d.gif|left|200px]]<br /><applet load="1t1d" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1t1d, resolution 1.51&Aring;" />
'''CRYSTAL STRUCTURE OF THE TETRAMERIZATION DOMAIN OF THE SHAKER POTASSIUM CHANNEL'''<br />
'''CRYSTAL STRUCTURE OF THE TETRAMERIZATION DOMAIN OF THE SHAKER POTASSIUM CHANNEL'''<br />
==Overview==
==Overview==
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The N-terminal, cytoplasmic tetramerization domain (T1) of voltage-gated, K+ channels encodes molecular determinants for subfamily-specific assembly, of alpha-subunits into functional tetrameric channels. Crystal structures, of T1 tetramers from Shaw and Shaker subfamilies reveal a common, four-layered scaffolding. Within layer 4, on the hypothetical, membrane-facing side of the tetramer, the Shaw T1 tetramer contains four, zinc ions; each is coordinated by a histidine and two cysteines from one, monomer and by one cysteine from an adjacent monomer. The amino acids, involved in coordinating the Zn2+ ion occur in a HX5CX20CC sequence motif, that is highly conserved among all Shab, Shaw and Shal subfamily members, but is not found in Shaker subfamily members. We demonstrate by, coimmunoprecipitation that a few characteristic residues in the subunit, interface are crucial for subfamily-specific tetramerization of the T1, domains.
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The N-terminal, cytoplasmic tetramerization domain (T1) of voltage-gated K+ channels encodes molecular determinants for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. Crystal structures of T1 tetramers from Shaw and Shaker subfamilies reveal a common four-layered scaffolding. Within layer 4, on the hypothetical membrane-facing side of the tetramer, the Shaw T1 tetramer contains four zinc ions; each is coordinated by a histidine and two cysteines from one monomer and by one cysteine from an adjacent monomer. The amino acids involved in coordinating the Zn2+ ion occur in a HX5CX20CC sequence motif that is highly conserved among all Shab, Shaw and Shal subfamily members, but is not found in Shaker subfamily members. We demonstrate by coimmunoprecipitation that a few characteristic residues in the subunit interface are crucial for subfamily-specific tetramerization of the T1 domains.
==About this Structure==
==About this Structure==
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1T1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T1D OCA].
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1T1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1D OCA].
==Reference==
==Reference==
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[[Category: Choe, S.]]
[[Category: Choe, S.]]
[[Category: Kreusch, A.]]
[[Category: Kreusch, A.]]
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[[Category: Pfaffinger, P.J.]]
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[[Category: Pfaffinger, P J.]]
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[[Category: Stevens, C.F.]]
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[[Category: Stevens, C F.]]
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[[Category: aplysia kv1.1]]
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[[Category: aplysia kv1 1]]
[[Category: potassium channels]]
[[Category: potassium channels]]
[[Category: proton transport]]
[[Category: proton transport]]
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[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:27:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:53 2008''

Revision as of 13:08, 21 February 2008


1t1d, resolution 1.51Å

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CRYSTAL STRUCTURE OF THE TETRAMERIZATION DOMAIN OF THE SHAKER POTASSIUM CHANNEL

Overview

The N-terminal, cytoplasmic tetramerization domain (T1) of voltage-gated K+ channels encodes molecular determinants for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. Crystal structures of T1 tetramers from Shaw and Shaker subfamilies reveal a common four-layered scaffolding. Within layer 4, on the hypothetical membrane-facing side of the tetramer, the Shaw T1 tetramer contains four zinc ions; each is coordinated by a histidine and two cysteines from one monomer and by one cysteine from an adjacent monomer. The amino acids involved in coordinating the Zn2+ ion occur in a HX5CX20CC sequence motif that is highly conserved among all Shab, Shaw and Shal subfamily members, but is not found in Shaker subfamily members. We demonstrate by coimmunoprecipitation that a few characteristic residues in the subunit interface are crucial for subfamily-specific tetramerization of the T1 domains.

About this Structure

1T1D is a Single protein structure of sequence from Aplysia californica. Full crystallographic information is available from OCA.

Reference

Zn2+-binding and molecular determinants of tetramerization in voltage-gated K+ channels., Bixby KA, Nanao MH, Shen NV, Kreusch A, Bellamy H, Pfaffinger PJ, Choe S, Nat Struct Biol. 1999 Jan;6(1):38-43. PMID:9886290

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