4mfv
From Proteopedia
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| - | {{STRUCTURE_4mfv|  PDB=4mfv  |  SCENE=  }}  | ||
| - | ===Crystal structure of human CTNNBL1(residues 33~563)=== | ||
| - | {{ABSTRACT_PUBMED_24598747}} | ||
| - | == | + | ==Crystal structure of human CTNNBL1(residues 33~563)== | 
| - | [[http://www.uniprot.org/uniprot/CTBL1_HUMAN CTBL1_HUMAN | + | <StructureSection load='4mfv' size='340' side='right'caption='[[4mfv]], [[Resolution|resolution]] 2.92Å' scene=''> | 
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mfv]] is a 2 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=4MFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MFV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.92Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mfv OCA], [https://pdbe.org/4mfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mfv RCSB], [https://www.ebi.ac.uk/pdbsum/4mfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mfv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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>  | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> | 
| - | [[Category:  | + | <div class="pdbe-citations 4mfv" style="background-color:#fffaf0;"></div> | 
| - | [[Category:  | + | == References == | 
| - | [[Category:  | + | <references/> | 
| - | [[Category: Kim | + | __TOC__ | 
| - | [[Category:  | + | </StructureSection> | 
| - | + | [[Category: Homo sapiens]] | |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ahn JW]] | ||
| + | [[Category: Kim KJ]] | ||
| + | [[Category: Kim S]] | ||
Current revision
Crystal structure of human CTNNBL1(residues 33~563)
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Categories: Homo sapiens | Large Structures | Ahn JW | Kim KJ | Kim S
