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4mfu

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==Crystal structure of human CTNNBL1(residues 77~563)==
==Crystal structure of human CTNNBL1(residues 77~563)==
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<StructureSection load='4mfu' size='340' side='right' caption='[[4mfu]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
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<StructureSection load='4mfu' size='340' side='right'caption='[[4mfu]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mfu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MFU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mfu]] 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=4MFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MFU FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mfv|4mfv]]</td></tr>
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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]] 2.744&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTNNBL1, C20orf33, PP8304 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4mfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mfu OCA], [https://pdbe.org/4mfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mfu RCSB], [https://www.ebi.ac.uk/pdbsum/4mfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mfu ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mfu OCA], [http://pdbe.org/4mfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mfu RCSB], [http://www.ebi.ac.uk/pdbsum/4mfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mfu ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CTBL1_HUMAN CTBL1_HUMAN]] Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated Ig class switching recombination (CSR). May induce apoptosis.<ref>PMID:12659813</ref> <ref>PMID:18722174</ref>
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[https://www.uniprot.org/uniprot/CTBL1_HUMAN CTBL1_HUMAN] Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated Ig class switching recombination (CSR). May induce apoptosis.<ref>PMID:12659813</ref> <ref>PMID:18722174</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The hPrp19-CDC5L complex plays a crucial role during human pre-mRNA splicing by catalytic activation of the spliceosome. In order to elucidate the molecular architecture of the hPrp19-CDC5L complex, the crystal structure of CTNNBL1, one of the major components of this complex, was determined. Unlike canonical ARM-repeat proteins such as beta-catenin and importin-alpha, CTNNBL1 was found to contain a twisted and extended ARM-repeat structure at the C-terminal domain and, more importantly, the protein formed a stable dimer. A highly negatively charged patch formed in the N-terminal ARM-repeat domain of CTNNBL1 provides a binding site for CDC5L, a binding partner of the protein in the hPrp19-CDC5L complex, and these two proteins form a complex with a stoichiometry of 2:2. These findings not only present the crystal structure of a novel ARM-repeat protein, CTNNBL1, but also provide insights into the detailed molecular architecture of the hPrp19-CDC5L complex.
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Structural insights into the novel ARM-repeat protein CTNNBL1 and its association with the hPrp19-CDC5L complex.,Ahn JW, Kim S, Kim EJ, Kim YJ, Kim KJ Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):780-8. doi:, 10.1107/S139900471303318X. Epub 2014 Feb 22. PMID:24598747<ref>PMID:24598747</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4mfu" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Ahn, J W]]
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[[Category: Large Structures]]
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[[Category: Kim, K J]]
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[[Category: Ahn JW]]
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[[Category: Kim, S]]
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[[Category: Kim KJ]]
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[[Category: Arm repeat]]
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[[Category: Kim S]]
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[[Category: Gene regulation]]
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Current revision

Crystal structure of human CTNNBL1(residues 77~563)

PDB ID 4mfu

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