1k1a

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(New page: 200px<br /> <applet load="1k1a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1a, resolution 1.86&Aring;" /> '''Crystal structure o...)
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'''Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family'''<br />
'''Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family'''<br />
==Overview==
==Overview==
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IkappaB proteins associate with the transcription factor NF-kappaB via, their ankyrin repeat domain. Bcl-3 is an unusual IkappaB protein because, it is primarily nucleoplasmic and can lead to enhanced NF-kappaB-dependent, transcription, unlike the prototypical IkappaB protein IkappaBalpha, which, inhibits NF-kappaB activity by retaining it in the cytoplasm. Here we, report the 1.9 A crystal structure of the ankyrin repeat domain of human, Bcl-3 and compare it with that of IkappaBalpha bound to NF-kappaB. The two, structures are highly similar over the central ankyrin repeats but differ, in the N-terminal repeat and at the C-terminus, where Bcl-3 contains a, seventh repeat in place of the acidic PEST region of IkappaBalpha., Differences between the two structures suggest why Bcl-3 differs from, IkappaBalpha in selectivity towards various NF-kappaB species, why Bcl-3, but not IkappaBalpha can associate with its NF-kappaB partner bound to, DNA, and why two molecules of Bcl-3 but only one of IkappaBalpha can bind, to its NF-kappaB partner. Comparison of the two structures thus provides, an insight into the functional diversity of IkappaB proteins.
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IkappaB proteins associate with the transcription factor NF-kappaB via their ankyrin repeat domain. Bcl-3 is an unusual IkappaB protein because it is primarily nucleoplasmic and can lead to enhanced NF-kappaB-dependent transcription, unlike the prototypical IkappaB protein IkappaBalpha, which inhibits NF-kappaB activity by retaining it in the cytoplasm. Here we report the 1.9 A crystal structure of the ankyrin repeat domain of human Bcl-3 and compare it with that of IkappaBalpha bound to NF-kappaB. The two structures are highly similar over the central ankyrin repeats but differ in the N-terminal repeat and at the C-terminus, where Bcl-3 contains a seventh repeat in place of the acidic PEST region of IkappaBalpha. Differences between the two structures suggest why Bcl-3 differs from IkappaBalpha in selectivity towards various NF-kappaB species, why Bcl-3 but not IkappaBalpha can associate with its NF-kappaB partner bound to DNA, and why two molecules of Bcl-3 but only one of IkappaBalpha can bind to its NF-kappaB partner. Comparison of the two structures thus provides an insight into the functional diversity of IkappaB proteins.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1K1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K1A OCA].
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1K1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1A OCA].
==Reference==
==Reference==
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[[Category: Cramer, P.]]
[[Category: Cramer, P.]]
[[Category: Michel, F.]]
[[Category: Michel, F.]]
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[[Category: Mueller, C.W.]]
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[[Category: Mueller, C W.]]
[[Category: Petosa, C.]]
[[Category: Petosa, C.]]
[[Category: Siebenlist, U.]]
[[Category: Siebenlist, U.]]
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[[Category: nf-kappab transcription factors]]
[[Category: nf-kappab transcription factors]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:46:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:56 2008''

Revision as of 11:28, 21 February 2008


1k1a, resolution 1.86Å

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Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family

Contents

Overview

IkappaB proteins associate with the transcription factor NF-kappaB via their ankyrin repeat domain. Bcl-3 is an unusual IkappaB protein because it is primarily nucleoplasmic and can lead to enhanced NF-kappaB-dependent transcription, unlike the prototypical IkappaB protein IkappaBalpha, which inhibits NF-kappaB activity by retaining it in the cytoplasm. Here we report the 1.9 A crystal structure of the ankyrin repeat domain of human Bcl-3 and compare it with that of IkappaBalpha bound to NF-kappaB. The two structures are highly similar over the central ankyrin repeats but differ in the N-terminal repeat and at the C-terminus, where Bcl-3 contains a seventh repeat in place of the acidic PEST region of IkappaBalpha. Differences between the two structures suggest why Bcl-3 differs from IkappaBalpha in selectivity towards various NF-kappaB species, why Bcl-3 but not IkappaBalpha can associate with its NF-kappaB partner bound to DNA, and why two molecules of Bcl-3 but only one of IkappaBalpha can bind to its NF-kappaB partner. Comparison of the two structures thus provides an insight into the functional diversity of IkappaB proteins.

Disease

Known disease associated with this structure: Leukemia/lymphoma, B-cell OMIM:[109560]

About this Structure

1K1A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family., Michel F, Soler-Lopez M, Petosa C, Cramer P, Siebenlist U, Muller CW, EMBO J. 2001 Nov 15;20(22):6180-90. PMID:11707390

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