Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining.

ABSTRACT: The solution structure and dynamics of the BRCT domain from human DNA polymerase mu, implicated in repair of chromosome breaks by nonhomologous end joining (NHEJ), has been determined using NMR methods. BRCT domains are typically involved in protein-protein interactions between factors required for the cellular response to DNA damage. The pol mu BRCT domain is atypical in that, unlike other reported BRCT structures, the pol mu BRCT is neither part of a tandem grouping, nor does it appear to form stable homodimers. Although the sequence of the pol mu BRCT domain has some unique characteristics, particularly the presence of >10% proline residues, it forms the characteristic alphabetaalpha sandwich, in which three alpha helices are arrayed around a central four-stranded beta-sheet. The struct

SUBMITTER: DeRose EF 

PROVIDER: S-EPMC2653216 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature