Structural insights into the novel ARM-repeat protein CTNNBL1 and its association with 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, Jae-Woo; Kim, Sangwoo; Kim, Eun-Jung; Kim, Yeo-Jin; Kim, Kyung-Jin
- PRP19P-ASSOCIATED COMPLEX; U-BOX; SPLICEOSOME; RNA; PRP19; ACTIVATION; NUCLEAR; STOICHIOMETRY; EXPRESSION; FAMILY
- Issue Date
- ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.70, no., pp.780 - 788
- 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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