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4hm9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1001Å</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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | [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> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4hm9" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of full-length human catenin-beta-like 1
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Categories: Homo sapiens | Large Structures | Du Z | Huang X | Wang G | Wu Y
