4mfu

</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=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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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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