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| | ==NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN XRCC1-N-TERMINAL DOMAIN== | | ==NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN XRCC1-N-TERMINAL DOMAIN== |
| - | <StructureSection load='1xna' size='340' side='right' caption='[[1xna]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1xna' size='340' side='right'caption='[[1xna]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xna]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XNA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xna]] 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=1XNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XNA FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XRCC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1xna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xna OCA], [http://pdbe.org/1xna PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xna RCSB], [http://www.ebi.ac.uk/pdbsum/1xna PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xna 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=1xna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xna OCA], [https://pdbe.org/1xna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xna RCSB], [https://www.ebi.ac.uk/pdbsum/1xna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xna ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/XRCC1_HUMAN XRCC1_HUMAN]] Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. | + | [https://www.uniprot.org/uniprot/XRCC1_HUMAN XRCC1_HUMAN] Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Marintchev, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Mullen, G P]] | + | [[Category: Marintchev A]] |
| - | [[Category: 3d nmr]] | + | [[Category: Mullen GP]] |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna polymerase-beta binding]]
| + | |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Single-strand break dna binding]]
| + | |
| - | [[Category: Xrcc1]]
| + | |
| Structural highlights
Function
XRCC1_HUMAN Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
XRCC1 functions in the repair of single-strand DNA breaks in mammalian cells and forms a repair complex with beta-Pol, ligase III and PARP. Here we describe the NMR solution structure of the XRCC1 N-terminal domain (XRCC1 NTD). The structural core is a beta-sandwich with beta-strands connected by loops, three helices and two short two-stranded beta-sheets at each connection side. We show, for the first time, that the XRCC1 NTD specifically binds single-strand break DNA (gapped and nicked). We also show that the XRCC1 NTD binds a gapped DNA-beta-Pol complex. The DNA binding and beta-Pol binding surfaces were mapped by NMR and found to be well suited for interaction with single-strand gap DNA containing a 90 degrees bend, and for simultaneously making contacts with the palm-thumb of beta-Pol in a ternary complex. The findings suggest a mechanism for preferential binding of the XRCC1 NTD to flexible single-strand break DNA.
Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.,Marintchev A, Mullen MA, Maciejewski MW, Pan B, Gryk MR, Mullen GP Nat Struct Biol. 1999 Sep;6(9):884-93. PMID:10467102[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marintchev A, Mullen MA, Maciejewski MW, Pan B, Gryk MR, Mullen GP. Solution structure of the single-strand break repair protein XRCC1 N-terminal domain. Nat Struct Biol. 1999 Sep;6(9):884-93. PMID:10467102 doi:10.1038/12347
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