4CB8

Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin alpha

Summary for 4CB8

• Entry DOI: 10.2210/pdb4cb8/pdb
• Related: 4CB9 4CBA
• Descriptor: BETA-CATENIN-LIKE PROTEIN 1, SULFATE ION (3 entities in total)
• Functional Keywords: apoptosis, import, aid, deaminase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus: Q8WYA6
• Total number of polymer chains: 1
• Total formula weight: 57407.83

Authors

Ganesh, K.,vanMaldegem, F.,Telerman, S.B.,Simpson, P.,Johnson, C.M.,Williams, R.L.,Neuberger, M.S.,Rada, C. (deposition date: 2013-10-10, release date: 2013-12-04, Last modification date: 2024-05-08)

Primary citation

Ganesh, K.,Maldegem, F.V.,Telerman, S.B.,Simpson, P.,Johnson, C.M.,Williams, R.L.,Neuberger, M.S.,Rada, C.
Structural and Mutational Analysis Reveals that Ctnnbl1 Binds Nlss in a Manner Distinct from that of its Closest Armadillo-Relative, Karyopherin Alpha
FEBS Lett., 588:21-, 2014

PubMed Abstract: CTNNBL1 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-α. 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-α 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-αs.

PubMed: 24269683
DOI: 10.1016/J.FEBSLET.2013.11.013

Experimental method

X-RAY DIFFRACTION (2.9 Å)