Structural basis for recruitment of BRCA2 by PALB2

Oliver, Antony W, Swift, Sally, Lord, Christopher J, Ashworth, Alan and Pearl, Laurence H (2009) Structural basis for recruitment of BRCA2 by PALB2. EMBO Reports, 10 (9). pp. 990-996. ISSN 1469-221X

Full text not available from this repository.


The breast cancer 2, early onset protein (BRCA2) is central to the repair of DNA damage by homologous recombination. BRCA2 recruits the recombinase RAD51 to sites of damage, regulates its assembly into nucleoprotein filaments and thereby promotes homologous recombination. Localization of BRCA2 to nuclear foci requires its association with the partner and localizer of BRCA2 (PALB2), mutations in which are associated with cancer predisposition, as well as subtype N of Fanconi anaemia. We have determined the structure of the PALB2 carboxy terminal beta-propeller domain in complex with a BRCA2 peptide. The structure shows the molecular determinants of this important protein protein interaction and explains the effects of both cancer associated truncating mutants in PALB2 and missense mutations in the amino terminal region of BRCA2.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Depositing User: Antony Oliver
Date Deposited: 06 Feb 2012 21:24
Last Modified: 03 Apr 2012 11:25
📧 Request an update