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| | ==X-ray crystal structure of the DNA ligase III-alpha BRCT domain.== | | ==X-ray crystal structure of the DNA ligase III-alpha BRCT domain.== |
| - | <StructureSection load='3pc7' size='340' side='right' caption='[[3pc7]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='3pc7' size='340' side='right'caption='[[3pc7]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pc7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PC7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pc7]] 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=3PC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PC7 FirstGlance]. <br> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pc6|3pc6]], [[3pc8|3pc8]], [[3qvg|3qvg]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LIG3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3pc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pc7 OCA], [https://pdbe.org/3pc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pc7 RCSB], [https://www.ebi.ac.uk/pdbsum/3pc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pc7 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_ligase_(ATP) DNA ligase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.1 6.5.1.1] </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=3pc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pc7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pc7 RCSB], [http://www.ebi.ac.uk/pdbsum/3pc7 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DNLI3_HUMAN DNLI3_HUMAN] Interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3pc7" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[DNA ligase|DNA ligase]] | + | *[[DNA ligase 3D structures|DNA ligase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Cuneo, M J]] | + | [[Category: Large Structures]] |
| - | [[Category: Krahn, J M]] | + | [[Category: Cuneo MJ]] |
| - | [[Category: London, R E]] | + | [[Category: Krahn JM]] |
| - | [[Category: Brct domain]] | + | [[Category: London RE]] |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Dna repair]]
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| - | [[Category: Ligase]]
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| - | [[Category: Protein:protein interaction]]
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| - | [[Category: Xrcc1 brct2 domain]]
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| Structural highlights
Function
DNLI3_HUMAN Interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.
Publication Abstract from PubMed
The ultimate step common to almost all DNA repair pathways is the ligation of the nicked intermediate to form contiguous double-stranded DNA. In the mammalian nucleotide and base excision repair pathways, the ligation step is carried out by ligase III-alpha. For efficient ligation, ligase III-alpha is constitutively bound to the scaffolding protein XRCC1 through interactions between the C-terminal BRCT domains of each protein. Although structural data for the individual domains has been available, no structure of the complex has been determined and several alternative proposals for this interaction have been advanced. Interpretation of the models is complicated by the formation of homodimers that, depending on the model, may either contribute to, or compete with heterodimer formation. We report here the structures of both homodimer complexes as well as the heterodimer complex. Structural characterization of the heterodimer formed from a longer XRCC1 BRCT domain construct, including residues comprising the interdomain linker region, revealed an expanded heterodimer interface with the ligase III-alpha BRCT domain. This enhanced linker-mediated binding interface plays a significant role in the determination of heterodimer/homodimer selectivity. These data provide fundamental insights into the structural basis of BRCT-mediated dimerization, and resolve questions related to the organization of this important repair complex.
The structural basis for partitioning of the XRCC1/DNA ligase III-alpha BRCT-mediated dimer complexes.,Cuneo MJ, Gabel SA, Krahn JM, Ricker MA, London RE Nucleic Acids Res. 2011 Sep 1;39(17):7816-27. Epub 2011 Jun 7. PMID:21652643[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cuneo MJ, Gabel SA, Krahn JM, Ricker MA, London RE. The structural basis for partitioning of the XRCC1/DNA ligase III-alpha BRCT-mediated dimer complexes. Nucleic Acids Res. 2011 Sep 1;39(17):7816-27. Epub 2011 Jun 7. PMID:21652643 doi:10.1093/nar/gkr419
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