Linking up and interacting with BRCT domains

Watts, Felicity Z and Brissett, Nigel C (2010) Linking up and interacting with BRCT domains. DNA Repair, 9 (2). pp. 103-8. ISSN 1568-7864

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Abstract

BRCT domains are present in an ever expanding family of proteins that includes many DNA repair and checkpoint proteins. The most prominent member of the BRCT family is BRCA1, mutations in which are responsible for a high proportion of breast and ovarian cancers. BRCT domains act as protein-protein interaction modules and facilitate the formation of hetero- and homo-oligomers. The domains occur either singly or in pairs, with up to eight domains in a single protein. When in pairs the domains are separated by a short inter-BRCT linker. Numerous crystal structures have been determined for BRCT domains from a range of different proteins, which indicate that the overall structure of the BRCT domains is generally well conserved. In contrast, the positions and structures of the linker regions are more varied, as are the roles of the linkers. Here, we describe the protein-protein interactions involving three different inter-BRCT linker regions, those of DNA ligase IV (LigIV), Schizosaccharomyces pombe Crb2 and human 53BP1.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Depositing User: Felicity Watts
Date Deposited: 06 Feb 2012 21:23
Last Modified: 17 Jul 2013 11:46
URI: http://sro.sussex.ac.uk/id/eprint/31078
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