1k1a
From Proteopedia
(New page: 200px<br /> <applet load="1k1a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1a, resolution 1.86Å" /> '''Crystal structure o...) |
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caption="1k1a, resolution 1.86Å" /> | caption="1k1a, resolution 1.86Å" /> | ||
'''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== | ||
- | IkappaB proteins associate with the transcription factor NF-kappaB via | + | 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== | ||
- | 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:// | + | 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.]] | ||
- | [[Category: Mueller, C | + | [[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]] | ||
- | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 13:28:56 2008