4MFV
Crystal structure of human CTNNBL1(residues 33~563)
Summary for 4MFV
| Entry DOI | 10.2210/pdb4mfv/pdb |
| Related | 4MFU |
| Descriptor | Beta-catenin-like protein 1 (1 entity in total) |
| Functional Keywords | arm repeats, gene regulation |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Nucleus. Isoform 2: Cytoplasm : Q8WYA6 |
| Total number of polymer chains | 2 |
| Total formula weight | 123360.75 |
| Authors | |
| Primary citation | Ahn, J.W.,Kim, S.,Kim, E.J.,Kim, Y.J.,Kim, K.J. Structural insights into the novel ARM-repeat protein CTNNBL1 and its association with the hPrp19-CDC5L complex Acta Crystallogr.,Sect.D, 70:780-788, 2014 Cited by PubMed Abstract: 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. PubMed: 24598747DOI: 10.1107/S139900471303318X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.92 Å) |
Structure validation
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