3pg6

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==The carboxyl terminal domain of human deltex 3-like==
==The carboxyl terminal domain of human deltex 3-like==
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<StructureSection load='3pg6' size='340' side='right' caption='[[3pg6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='3pg6' size='340' side='right'caption='[[3pg6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pg6]] is a 4 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=3PG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PG6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pg6]] is a 4 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=3PG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PG6 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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BBAP, DTX3L ([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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=3pg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pg6 OCA], [http://pdbe.org/3pg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pg6 RCSB], [http://www.ebi.ac.uk/pdbsum/3pg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pg6 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=3pg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pg6 OCA], [https://pdbe.org/3pg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pg6 RCSB], [https://www.ebi.ac.uk/pdbsum/3pg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pg6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DTX3L_HUMAN DTX3L_HUMAN]] Ubiquitin ligase that mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.<ref>PMID:12670957</ref> <ref>PMID:19818714</ref> <ref>PMID:23230272</ref>
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[https://www.uniprot.org/uniprot/DTX3L_HUMAN DTX3L_HUMAN] Ubiquitin ligase that mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.<ref>PMID:12670957</ref> <ref>PMID:19818714</ref> <ref>PMID:23230272</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human Deltex 3-like (DTX3L) is a member of the Deltex family of proteins. Initially identified as a B-lymphoma and BAL-associated protein, DTX3L is an E3 ligase that regulates subcellular localization of its partner protein, BAL, by a dynamic nucleocytoplasmic trafficking mechanism. Unlike other members of the Deltex family of proteins, DTX3L lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex proteins, and instead contains other unique N-terminal domains. The C-terminal domains are, however, homologous with other members of the Deltex family of proteins; these include a RING domain and a previously unidentified C-terminal domain. In this study, we report the high-resolution crystal structure of this previously uncharacterized C-terminal domain of human DTX3L, which we term the Deltex C-terminal domain.
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Fold of the conserved DTC domain in Deltex proteins.,Obiero J, Walker JR, Dhe-Paganon S Proteins. 2012 May;80(5):1495-9. doi: 10.1002/prot.24054. Epub 2012 Mar 13. PMID:22411408<ref>PMID:22411408</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 3pg6" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H]]
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[[Category: Large Structures]]
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[[Category: Bountra, C]]
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[[Category: Arrowsmith CH]]
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[[Category: Dhe-Paganon, S]]
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[[Category: Bountra C]]
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[[Category: Edwards, A M]]
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[[Category: Dhe-Paganon S]]
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[[Category: Kania, J]]
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[[Category: Edwards AM]]
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[[Category: Obiero, J]]
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[[Category: Kania J]]
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[[Category: Structural genomic]]
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[[Category: Obiero J]]
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[[Category: Schuler, H]]
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[[Category: Schuler H]]
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[[Category: Walker, J R]]
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[[Category: Walker JR]]
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[[Category: Weigelt, J]]
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[[Category: Weigelt J]]
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[[Category: Chromatin regulator]]
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[[Category: Dna-damage]]
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[[Category: Ligase]]
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[[Category: Metal-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphorylation]]
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[[Category: Sgc]]
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[[Category: Ubl conjugation pathway]]
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[[Category: Zinc-finger]]
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Current revision

The carboxyl terminal domain of human deltex 3-like

PDB ID 3pg6

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