1ikn

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(New page: 200px<br /> <applet load="1ikn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ikn, resolution 2.300&Aring;" /> '''IKAPPABALPHA/NF-KA...)
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[[Image:1ikn.gif|left|200px]]<br />
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[[Image:1ikn.gif|left|200px]]<br /><applet load="1ikn" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1ikn" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1ikn, resolution 2.300&Aring;" />
caption="1ikn, resolution 2.300&Aring;" />
'''IKAPPABALPHA/NF-KAPPAB COMPLEX'''<br />
'''IKAPPABALPHA/NF-KAPPAB COMPLEX'''<br />
==Overview==
==Overview==
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IkappaBalpha regulates the transcription factor NF-kappaB through the, formation of stable IkappaBalpha/NF-kappaB complexes. Prior to induction, IkappaBalpha retains NF-kappaB in the cytoplasm until the NF-kappaB, activation signal is received. After activation, NF-kappaB is removed from, gene promoters through association with nuclear IkappaBalpha, restoring, the preinduction state. The 2.3 A crystal structure of IkappaBalpha in, complex with the NF-kappaB p50/p65 heterodimer reveals mechanisms of these, inhibitory activities. The presence of IkappaBalpha allows large en bloc, movement of the NF-kappaB p65 subunit amino-terminal domain. This, conformational change induces allosteric inhibition of NF-kappaB DNA, binding. Amino acid residues immediately preceding the nuclear, localization signals of both NF-kappaB p50 and p65 subunits are tethered, to the IkappaBalpha amino-terminal ankyrin repeats, impeding NF-kappaB, from nuclear import machinery recognition.
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IkappaBalpha regulates the transcription factor NF-kappaB through the formation of stable IkappaBalpha/NF-kappaB complexes. Prior to induction, IkappaBalpha retains NF-kappaB in the cytoplasm until the NF-kappaB activation signal is received. After activation, NF-kappaB is removed from gene promoters through association with nuclear IkappaBalpha, restoring the preinduction state. The 2.3 A crystal structure of IkappaBalpha in complex with the NF-kappaB p50/p65 heterodimer reveals mechanisms of these inhibitory activities. The presence of IkappaBalpha allows large en bloc movement of the NF-kappaB p65 subunit amino-terminal domain. This conformational change induces allosteric inhibition of NF-kappaB DNA binding. Amino acid residues immediately preceding the nuclear localization signals of both NF-kappaB p50 and p65 subunits are tethered to the IkappaBalpha amino-terminal ankyrin repeats, impeding NF-kappaB from nuclear import machinery recognition.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1IKN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IKN OCA].
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1IKN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IKN OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Ghosh, G.]]
[[Category: Ghosh, G.]]
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[[Category: Huang, D.B.]]
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[[Category: Huang, D B.]]
[[Category: Huxford, T.]]
[[Category: Huxford, T.]]
[[Category: Malek, S.]]
[[Category: Malek, S.]]
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:30:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:55 2008''

Revision as of 11:12, 21 February 2008


1ikn, resolution 2.300Å

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IKAPPABALPHA/NF-KAPPAB COMPLEX

Contents

Overview

IkappaBalpha regulates the transcription factor NF-kappaB through the formation of stable IkappaBalpha/NF-kappaB complexes. Prior to induction, IkappaBalpha retains NF-kappaB in the cytoplasm until the NF-kappaB activation signal is received. After activation, NF-kappaB is removed from gene promoters through association with nuclear IkappaBalpha, restoring the preinduction state. The 2.3 A crystal structure of IkappaBalpha in complex with the NF-kappaB p50/p65 heterodimer reveals mechanisms of these inhibitory activities. The presence of IkappaBalpha allows large en bloc movement of the NF-kappaB p65 subunit amino-terminal domain. This conformational change induces allosteric inhibition of NF-kappaB DNA binding. Amino acid residues immediately preceding the nuclear localization signals of both NF-kappaB p50 and p65 subunits are tethered to the IkappaBalpha amino-terminal ankyrin repeats, impeding NF-kappaB from nuclear import machinery recognition.

Disease

Known diseases associated with this structure: Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency OMIM:[164008]

About this Structure

1IKN is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation., Huxford T, Huang DB, Malek S, Ghosh G, Cell. 1998 Dec 11;95(6):759-70. PMID:9865694

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