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5vdc

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Current revision (14:32, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5vdc' size='340' side='right'caption='[[5vdc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5vdc' size='340' side='right'caption='[[5vdc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vdc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VDC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VDC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vdc]] 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=5VDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VDC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 1.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DPF2, BAF45D, REQ, UBID4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5vdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vdc OCA], [http://pdbe.org/5vdc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vdc RCSB], [http://www.ebi.ac.uk/pdbsum/5vdc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vdc ProSAT]</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=5vdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vdc OCA], [https://pdbe.org/5vdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vdc RCSB], [https://www.ebi.ac.uk/pdbsum/5vdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vdc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/REQU_HUMAN REQU_HUMAN]] May be a transcription factor required for the apoptosis response following survival factor withdrawal from myeloid cells. Might also have a role in the development and maturation of lymphoid cells.
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[https://www.uniprot.org/uniprot/REQU_HUMAN REQU_HUMAN] May be a transcription factor required for the apoptosis response following survival factor withdrawal from myeloid cells. Might also have a role in the development and maturation of lymphoid cells.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Double plant homeodomain finger 2 (DPF2) is a highly evolutionarily conserved member of the d4 protein family that is ubiquitously expressed in human tissues and was recently shown to inhibit the myeloid differentiation of hematopoietic stem/progenitor and acute myelogenous leukemia cells. Here, we present the crystal structure of the tandem plant homeodomain finger domain of human DPF2 at 1.6-A resolution. We show that DPF2 interacts with the acetylated tails of both histones 3 and 4 via bipartite binding pockets on the DPF2 surface. Blocking these interactions through targeted mutagenesis of DPF2 abolishes its recruitment to target chromatin regions as well as its ability to prevent myeloid differentiation in vivo. Our findings suggest that the histone binding of DPF2 plays an important regulatory role in the transcriptional program that drives myeloid differentiation.
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Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.,Huber FM, Greenblatt SM, Davenport AM, Martinez C, Xu Y, Vu LP, Nimer SD, Hoelz A Proc Natl Acad Sci U S A. 2017 Jun 6;114(23):6016-6021. doi:, 10.1073/pnas.1700328114. Epub 2017 May 22. PMID:28533407<ref>PMID:28533407</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 5vdc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Davenport, A M]]
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[[Category: Davenport AM]]
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[[Category: Hoelz, A]]
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[[Category: Hoelz A]]
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[[Category: Huber, F M]]
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[[Category: Huber FM]]
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[[Category: Aml]]
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[[Category: Gene regulation]]
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[[Category: Histone reader]]
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[[Category: Myeloid differentiation]]
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[[Category: Tandem phd finger]]
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Current revision

Crystal structure of the human DPF2 tandem PHD finger domain

PDB ID 5vdc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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