4l7x
From Proteopedia
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| - | {{STRUCTURE_4l7x| PDB=4l7x | SCENE= }} | ||
| - | ===Crystal structure of the DIDO PHD finger in complex with H3K4me3=== | ||
| - | {{ABSTRACT_PUBMED_23831028}} | ||
| - | == | + | ==Crystal structure of the DIDO PHD finger in complex with H3K4me3== |
| - | [[4l7x]] is a 2 chain structure with sequence from [ | + | <StructureSection load='4l7x' size='340' side='right'caption='[[4l7x]], [[Resolution|resolution]] 1.35Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4l7x]] is a 2 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=4L7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L7X FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4l7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7x OCA], [https://pdbe.org/4l7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l7x RCSB], [https://www.ebi.ac.uk/pdbsum/4l7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l7x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DIDO1_HUMAN DIDO1_HUMAN] Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor.<ref>PMID:16127461</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Death Inducer Obliterator 3 (Dido3) is implicated in the maintenance of stem cell genomic stability and tumorigenesis. Here, we show that Dido3 regulates the expression of stemness genes in embryonic stem cells through its plant homeodomain (PHD) finger. Binding of Dido3 PHD to histone H3K4me3 is disrupted by threonine phosphorylation that triggers Dido3 translocation from chromatin to the mitotic spindle. The crystal structure of Dido3 PHD in complex with H3K4me3 reveals an atypical aromatic-cage-like binding site that contains a histidine residue. Biochemical, structural, and mutational analyses of the binding mechanism identified the determinants of specificity and affinity and explained the inability of homologous PHF3 to bind H3K4me3. Together, our findings reveal a link between the transcriptional control in embryonic development and regulation of cell division. | ||
| - | + | Dido3 PHD Modulates Cell Differentiation and Division.,Gatchalian J, Futterer A, Rothbart SB, Tong Q, Rincon-Arano H, Sanchez de Diego A, Groudine M, Strahl BD, Martinez-A C, van Wely KH, Kutateladze TG Cell Rep. 2013 Jul 11;4(1):148-58. doi: 10.1016/j.celrep.2013.06.014. Epub 2013, Jul 3. PMID:23831028<ref>PMID:23831028</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4l7x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Gatchalian J]] |
| - | [[Category: | + | [[Category: Kutateladze TG]] |
| - | [[Category: | + | [[Category: Tong Q]] |
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Current revision
Crystal structure of the DIDO PHD finger in complex with H3K4me3
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