Structural highlights
Function[CTBL1_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 PubMedCTNNBL1 is a spliceosome-associated protein that binds nuclear localization signals (NLSs) in splice factors CDC5L and Prp31 as well as the antibody diversifying enzyme AID. Here, crystal structures of human CTNNBL1 reveal a distinct structure from its closest homologue karyopherin-alphas. CTNNBL1 comprises a HEAT-like domain (including a nuclear export signal), a central armadillo domain, and a coiled-coil C-terminal domain. Structure-guided mutations of the region homologous to the karyopherin-alpha NLS-binding site fail to disrupt CTNNBL1-NLS interactions. Our results identify CTNNBL1 as a unique selective NLS-binding protein with striking differences from karyopherin-alphas. Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin alpha,Ganesh K, van Maldegem F, Telerman SB, Simpson P, Johnson CM, Williams RL, Neuberger MS, Rada C FEBS Lett. 2013 Nov 20. pii: S0014-5793(13)00847-8. doi:, 10.1016/j.febslet.2013.11.013. PMID:24269683[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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