Structural insights into the novel ARM-repeat protein CTNNBL1 and its association with the hPrp19-CDC5L complex.
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 β-catenin ... and importin-α, 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.
Mesh Terms:
Apoptosis Regulatory Proteins, Armadillo Domain Proteins, Cell Cycle Proteins, DNA Repair Enzymes, Humans, Membrane Glycoproteins, Nuclear Proteins, Protein Binding, Protein Multimerization, RNA Precursors, RNA Splicing, RNA-Binding Proteins, Tandem Repeat Sequences
Apoptosis Regulatory Proteins, Armadillo Domain Proteins, Cell Cycle Proteins, DNA Repair Enzymes, Humans, Membrane Glycoproteins, Nuclear Proteins, Protein Binding, Protein Multimerization, RNA Precursors, RNA Splicing, RNA-Binding Proteins, Tandem Repeat Sequences
Acta Crystallogr. D Biol. Crystallogr.
Date: Mar. 01, 2014
PubMed ID: 24598747
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