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Structure paper

TitleOxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 107, Page 6805-6810, Year 2010
Publish dateOct 12, 2009 (structure data deposition date)
AuthorsCuneo, M.J. / London, R.E.
External linksProc. Natl. Acad. Sci. USA / PubMed:20351257
MethodsX-ray diffraction
Resolution2.349 - 2.95 Å
Structure data

PDB-3k75:
X-ray crystal structure of reduced XRCC1 bound to DNA pol beta catalytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-3k77:
X-ray crystal structure of XRCC1
Method: X-RAY DIFFRACTION / Resolution: 2.597 Å

PDB-3lqc:
X-ray crystal structure of oxidized XRCC1 bound to DNA pol beta Palm thumb domain
Method: X-RAY DIFFRACTION / Resolution: 2.349 Å

Chemicals

ChemComp-HOH:
WATER / Water

ChemComp-NA:
Unknown entry

ChemComp-CO3:
CARBONATE ION / Carbonate

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
KeywordsDNA BINDING PROTEIN / allosteric disulfide / XRCC1 / pol beta / DNA damage / DNA repair / Nucleus / Phosphoprotein / DNA replication / DNA synthesis / DNA-binding / DNA-directed DNA polymerase / Lyase / Magnesium / Metal-binding / Methylation / Nucleotidyltransferase / Transferase / DNA-BINDING PROTEIN / PROTEIN BINDING / base excision repair / scaffolding protein / Polymorphism / Ubl conjugation / Sodium

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