Holding damaged DNA together.

Nature structural biology ·Vol. 6 ·No. 9 ·1999-09-00 ·Pages 805-6

Rice PA

Abstract

The mammalian X-ray cross-complementing group 1 protein (XRCC1) is an important player in base excision repair of damaged DNA. Two new findings help to elucidate its role - biochemical data suggest that this multidomain protein interacts not only with three different enzymes, but also with the nicked DNA itself, and NMR data reveal the structure of the domain that interacts with both DNA polymerase beta and DNA.

MeSH Terms

DNA/genetics,metabolism DNA Damage/genetics DNA Ligase ATP DNA Ligases/metabolism DNA Polymerase beta/metabolism DNA Repair DNA-Binding Proteins/chemistry,metabolism Humans Models, Molecular Nuclear Magnetic Resonance, Biomolecular Poly(ADP-ribose) Polymerases/metabolism Poly-ADP-Ribose Binding Proteins Protein Binding Protein Conformation X-ray Repair Cross Complementing Protein 1 Xenopus Proteins

Chemicals

DNA-Binding Proteins Poly-ADP-Ribose Binding Proteins X-ray Repair Cross Complementing Protein 1 XRCC1 protein, human Xenopus Proteins DNA Poly(ADP-ribose) Polymerases DNA Polymerase beta DNA Ligases DNA Ligase ATP DNA ligase III alpha protein, Xenopus

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Rice P A

Article Info

Journal

Nature structural biology

Abbr.

Nat Struct Biol

ISSN

1072-8368

DOI

10.1038/12257

Published

1999-09-00

Pages

805-6

Language

English

Region

United States

NLM ID

9421566

Subset

Corrections

CommentOn

PMID: 10467102

External Links

PubMed source DOI: 10.1038/12257

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