4mfv
Crystal structure of human CTNNBL1(residues 33~563)
Structural highlights
FunctionCTBL1_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.[1] [2] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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