4HNM

Crystal structure of human catenin-beta-like 1 56 kDa fragment

Summary for 4HNM

• Entry DOI: 10.2210/pdb4hnm/pdb
• Descriptor: Beta-catenin-like protein 1 (1 entity in total)
• Functional Keywords: all alpha-helical, armadillo repeats, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q8WYA6
• Total number of polymer chains: 1
• Total formula weight: 57170.57

Authors

Du, Z.,Huang, X.,Wang, G.,Wu, Y. (deposition date: 2012-10-19, release date: 2013-07-31, Last modification date: 2024-10-16)

Primary citation

Huang, X.,Wang, G.,Wu, Y.,Du, Z.
The structure of full-length human CTNNBL1 reveals a distinct member of the armadillo-repeat protein family.
Acta Crystallogr.,Sect.D, 69:1598-1608, 2013

PubMed Abstract: Catenin-β-like protein 1 (CTNNBL1) is a highly conserved protein with multiple functions, one of which is to act as an interaction partner of the antibody-diversification enzyme activation-induced cytidine deaminase (AID) for its nuclear import and subnuclear trafficking. Here, the crystal structure of full-length human CTNNBL1 is reported. The protein contains six armadillo (ARM) repeats that pack into a superhelical ARM domain. This ARM domain is unique within the ARM protein family owing to the presence of several unusual structural features. Moreover, CTNNBL1 contains significant and novel non-ARM structures flanking both ends of the central ARM domain. A strong continuous hydrophobic core runs through the whole structure, indicating that the ARM and non-ARM structures fold together to form an integral structure. This structure defines a highly restrictive and discriminatory protein-binding groove that is not observed in other ARM proteins. The presence of a cluster of histidine residues in the groove implies a pH-sensitive histidine-mediated mechanism that may regulate protein binding activity. The many unique structural features of CTNNBL1 establish it as a distinct member of the ARM protein family. The structure provides critical insights into the molecular interactions between CTNNBL1 and its protein partners, especially AID.

PubMed: 23897482
DOI: 10.1107/S0907444913011360

Experimental method

X-RAY DIFFRACTION (2.9001 Å)