8hib

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Current revision (20:16, 11 December 2024) (edit) (undo)
 
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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=8hib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hib OCA], [https://pdbe.org/8hib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hib RCSB], [https://www.ebi.ac.uk/pdbsum/8hib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hib ProSAT]</span></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=8hib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hib OCA], [https://pdbe.org/8hib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hib RCSB], [https://www.ebi.ac.uk/pdbsum/8hib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hib ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/LDB1_HUMAN LDB1_HUMAN] Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Play a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state (By similarity).
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== Publication Abstract from PubMed ==
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The Wnt enhanceosome is responsible for transactivation of Wnt-responsive genes and a promising therapeutic target for treatment of numerous cancers with Adenomatous Polyposis Coli (APC) or beta-catenin mutations. How the Wnt enhanceosome is assembled remains poorly understood. Here we show that B-cell lymphoma 9 protein (BCL9), Pygopus (Pygo), LIM domain-binding protein 1 (LDB1) and single-stranded DNA-binding protein (SSBP) form a stable core complex within the Wnt enhanceosome. Their mutual interactions rely on a highly conserved N-terminal asparagine proline phenylalanine (NPF) motif of Pygo, through which the BCL9-Pygo complex binds to the LDB-SSBP core complex. Our crystal structure of a ternary complex comprising the N-terminus of human Pygo2, LDB1 and SSBP2 reveals a single LDB1-SSBP2 complex binding simultaneously to two Pygo2 molecules via their NPF motifs. These interactions critically depend on the NPF motifs which bind to a deep groove formed between LDB1 and SSBP2, potentially constituting a binding site for drugs blocking Wnt/beta-catenin signaling. Analysis of human cell lines lacking LDB or Pygo supports the functional relevance of the Pygo-LDB1-SSBP2 interaction for Wnt/beta-catenin-dependent transcription.
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Structural basis of the interaction between BCL9-Pygo and LDB-SSBP complexes in assembling the Wnt enhanceosome.,Wang H, Bienz M, Yan XX, Xu W Nat Commun. 2023 Jun 22;14(1):3702. doi: 10.1038/s41467-023-39439-9. PMID:37349336<ref>PMID:37349336</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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<div class="pdbe-citations 8hib" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

The crystal structure of Pygo2-LDB1-SSBP2 triple complex

PDB ID 8hib

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