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| | ==Zinc finger domain of the human DTX protein== | | ==Zinc finger domain of the human DTX protein== |
| - | <StructureSection load='6ir0' size='340' side='right'caption='[[6ir0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6ir0' size='340' side='right'caption='[[6ir0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ir0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IR0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ir0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IR0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </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=6ir0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ir0 OCA], [https://pdbe.org/6ir0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ir0 RCSB], [https://www.ebi.ac.uk/pdbsum/6ir0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ir0 ProSAT]</span></td></tr> |
| - | <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=6ir0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ir0 OCA], [http://pdbe.org/6ir0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ir0 RCSB], [http://www.ebi.ac.uk/pdbsum/6ir0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ir0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DTX2_HUMAN DTX2_HUMAN]] Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity. | + | [https://www.uniprot.org/uniprot/DTX2_HUMAN DTX2_HUMAN] Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RING-type E3 ubiquitin transferase]]
| + | [[Category: Miyamoto K]] |
| - | [[Category: Miyamoto, K]] | + | |
| - | [[Category: Dtx]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Ring finger]]
| + | |
| - | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
DTX2_HUMAN Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity.
Publication Abstract from PubMed
The Deltex (DTX) family is involved in ubiquitination and acts as Notch signaling modifiers for controlling cell fate determination. DTX promotes the development of the ubiquitin chain via its RING finger (DTX_RING). In this study, the solution structure of DTX_RING was determined using nuclear magnetic resonance (NMR). Moreover, by experiments with a metallochromic indicator, we spectrophotometrically estimated the stoichiometry of zinc ions and found that DTX_RING possesses zinc-binding capabilities. The Simple Modular Architecture Research Tool database predicted the structure of DTX_RING as a typical RING finger. However, the actual DTX_RING structure adopts a novel RING fold with a unique topology distinct from other RING fingers. We unveiled the position and the range of the DTX_RING active site at the atomic level. Artificial RING fingers (ARFs) are made by grafting active sites of the RING fingers onto cross-brace structure motifs. Therefore, the present structural analysis could be useful for designing a novel ARF.
Zinc finger domain of the human DTX protein adopts a unique RING fold.,Miyamoto K, Fujiwara Y, Saito K Protein Sci. 2019 Jun;28(6):1151-1156. doi: 10.1002/pro.3610. Epub 2019 Apr 12. PMID:30927328[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyamoto K, Fujiwara Y, Saito K. Zinc finger domain of the human DTX protein adopts a unique RING fold. Protein Sci. 2019 Jun;28(6):1151-1156. doi: 10.1002/pro.3610. Epub 2019 Apr 12. PMID:30927328 doi:http://dx.doi.org/10.1002/pro.3610
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