Holding damaged DNA together

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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 β and DNA.

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Figure 1: Model of the proposed ternary complex of the XRCC1 N-terminal domain (yellow) and DNA polymerase β (blue) with nicked or gapped DNA (red)8.
Figure 2: Cartoon of short-patch base excision repair.
Figure 3: Model of the primary sequence of XRCC1, and its interaction partners (not drawn to scale).

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