4hm9

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==Crystal structure of full-length human catenin-beta-like 1==
==Crystal structure of full-length human catenin-beta-like 1==
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<StructureSection load='4hm9' size='340' side='right' caption='[[4hm9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='4hm9' size='340' side='right'caption='[[4hm9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4hm9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HM9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HM9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4hm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HM9 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C20orf33, CTNNBL1, PP8304 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1001&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hm9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hm9 RCSB], [http://www.ebi.ac.uk/pdbsum/4hm9 PDBsum]</span></td></tr>
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<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>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CTBL1_HUMAN 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.<ref>PMID:12659813</ref> <ref>PMID:18722174</ref>
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Du, Z]]
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[[Category: Large Structures]]
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[[Category: Huang, X]]
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[[Category: Du Z]]
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[[Category: Wang, G]]
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[[Category: Huang X]]
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[[Category: Wu, Y]]
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[[Category: Wang G]]
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[[Category: All alpha-helical]]
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[[Category: Wu Y]]
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[[Category: Armadillo repeat]]
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[[Category: Protein transport]]
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Current revision

Crystal structure of full-length human catenin-beta-like 1

PDB ID 4hm9

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