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Structure paper

TitleThe structural basis for partitioning of the XRCC1/DNA ligase III-{alpha} BRCT-mediated dimer complexes.
Journal, issue, pagesNucleic Acids Res., Vol. 39, Page 7816-7827, Year 2011
Publish dateOct 21, 2010 (structure data deposition date)
AuthorsCuneo, M.J. / Gabel, S.A. / Krahn, J.M. / Ricker, M.A. / London, R.E.
External linksNucleic Acids Res. / PubMed:21652643
MethodsX-ray diffraction
Resolution1.65 - 2.31 Å
Structure data

PDB-3pc6:
X-ray crystal structure of the second XRCC1 BRCT domain.
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3pc7:
X-ray crystal structure of the DNA ligase III-alpha BRCT domain.
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-3pc8:
X-ray crystal structure of the heterodimeric complex of XRCC1 and DNA ligase III-alpha BRCT domains.
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-3qvg:
XRCC1 bound to DNA ligase
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / DNA repair / BRCT domain / Protein:protein interactions / DNA ligase III-alpha BRCT2 domain / LIGASE / XRCC1 BRCT2 domain / DNA BINDING PROTEIN/LIGASE / DNA BINDING PROTEIN - LIGASE complex / DNA BINDING PROTEIN-LIGASE complex / XRCC1 / DNA ligase III-alpha

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