4hm9

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hm9 OCA], [https://pdbe.org/4hm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hm9 RCSB], [https://www.ebi.ac.uk/pdbsum/4hm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hm9 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Catenin-beta-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.

The structure of full-length human CTNNBL1 reveals a distinct member of the armadillo-repeat protein family.,Huang X, Wang G, Wu Y, Du Z Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1598-608. doi:, 10.1107/S0907444913011360. Epub 2013 Jul 20. PMID:23897482<ref>PMID:23897482</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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