3v3l

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<StructureSection load='3v3l' size='340' side='right'caption='[[3v3l]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='3v3l' size='340' side='right'caption='[[3v3l]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v3l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V3L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v3l]] 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=3V3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V3L FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=V3L:2-O-(5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSYL)ADENOSINE+5-(DIHYDROGEN+PHOSPHATE)'>V3L</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]] 1.65&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=V3L:2-O-(5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSYL)ADENOSINE+5-(DIHYDROGEN+PHOSPHATE)'>V3L</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNF146 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3v3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3l OCA], [https://pdbe.org/3v3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3l RCSB], [https://www.ebi.ac.uk/pdbsum/3v3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3l 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=3v3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3l OCA], [https://pdbe.org/3v3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3l RCSB], [https://www.ebi.ac.uk/pdbsum/3v3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3l ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/RN146_HUMAN RN146_HUMAN]] Note=Defects in RNF146 are a cause of susceptibility to breast cancer.
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[https://www.uniprot.org/uniprot/RN146_HUMAN RN146_HUMAN] Note=Defects in RNF146 are a cause of susceptibility to breast cancer.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RN146_HUMAN RN146_HUMAN]] E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair.<ref>PMID:21478859</ref> <ref>PMID:21602803</ref> <ref>PMID:21799911</ref> <ref>PMID:21825151</ref> <ref>PMID:22267412</ref>
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[https://www.uniprot.org/uniprot/RN146_HUMAN RN146_HUMAN] E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair.<ref>PMID:21478859</ref> <ref>PMID:21602803</ref> <ref>PMID:21799911</ref> <ref>PMID:21825151</ref> <ref>PMID:22267412</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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: Cheng, Z]]
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[[Category: Cheng Z]]
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[[Category: Wang, Z]]
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[[Category: Wang Z]]
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[[Category: Xu, W]]
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[[Category: Xu W]]
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[[Category: Ligase]]
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Current revision

Crystal structure of human RNF146 WWE domain in complex with iso-ADPRibose

PDB ID 3v3l

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