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1k1b

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(New page: 200px<br /> <applet load="1k1b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1b, resolution 1.9&Aring;" /> '''Crystal structure of...)
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[[Image:1k1b.gif|left|200px]]<br />
 
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<applet load="1k1b" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k1b, resolution 1.9&Aring;" />
 
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'''Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family'''<br />
 
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==Overview==
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==Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family==
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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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<StructureSection load='1k1b' size='340' side='right'caption='[[1k1b]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1k1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1B FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1b OCA], [https://pdbe.org/1k1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1b RCSB], [https://www.ebi.ac.uk/pdbsum/1k1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1b ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/BCL3_HUMAN BCL3_HUMAN] Note=A chromosomal aberration involving BCL3 may be a cause of B-cell chronic lymphocytic leukemia (B-CLL). Translocation t(14;19)(q32;q13.1) with immunoglobulin gene regions.
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== Function ==
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[https://www.uniprot.org/uniprot/BCL3_HUMAN BCL3_HUMAN] Contributes to the regulation of transcriptional activation of NF-kappa-B target genes. In the cytoplasm, inhibits the nuclear translocation of the NF-kappa-B p50 subunit. In the nucleus, acts as transcriptional activator that promotes transcription of NF-kappa-B target genes. Contributes to the regulation of cell proliferation (By similarity).<ref>PMID:8453667</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k1/1k1b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k1b ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==Disease==
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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<ref>PMID:11707390</ref>
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Known disease associated with this structure: Leukemia/lymphoma, B-cell OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109560 109560]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1K1B 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=1K1B OCA].
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</div>
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<div class="pdbe-citations 1k1b" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11707390 11707390]
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cramer, P.]]
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[[Category: Cramer P]]
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[[Category: Michel, F.]]
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[[Category: Michel F]]
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[[Category: Mueller, C.W.]]
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[[Category: Mueller CW]]
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[[Category: Petosa, C.]]
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[[Category: Petosa C]]
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[[Category: Siebenlist, U.]]
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[[Category: Siebenlist U]]
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[[Category: Soler-Lopez, M.]]
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[[Category: Soler-Lopez M]]
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[[Category: bcl-3]]
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[[Category: ikappab proteins]]
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[[Category: nf-kappab transcription factors]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:46:27 2007''
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Current revision

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

PDB ID 1k1b

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