1n0w

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1n0w, resolution 1.70Å

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Crystal structure of a RAD51-BRCA2 BRC repeat complex

Contents

Overview

The breast cancer susceptibility protein BRCA2 controls the function of, RAD51, a recombinase enzyme, in pathways for DNA repair by homologous, recombination. We report here the structure of a complex between an, evolutionarily conserved sequence in BRCA2 (the BRC repeat) and the, RecA-homology domain of RAD51. The BRC repeat mimics a motif in RAD51 that, serves as an interface for oligomerization between individual RAD51, monomers, thus enabling BRCA2 to control the assembly of the RAD51, nucleoprotein filament, which is essential for strand-pairing reactions, during DNA recombination. The RAD51 oligomerization motif is highly, conserved among RecA-like recombinases, highlighting a common evolutionary, origin for the mechanism of nucleoprotein filament formation, mirrored in, the BRC repeat. Cancer-associated mutations that affect the BRC repeat, disrupt its predicted interaction with RAD51, yielding structural insight, into mechanisms for cancer susceptibility.

Disease

Known diseases associated with this structure: Breast cancer 2, early onset OMIM:[600185], Breast cancer, male, susceptibility to OMIM:[600185], Breast cancer, susceptibility to OMIM:[179617], Fanconi anemia, complementation group D1 OMIM:[600185], Fanconi anemia, complementation group D2 OMIM:[227646], Pancreatic cancer OMIM:[600185], Prostate cancer OMIM:[600185], Wilms tumor OMIM:[600185]

About this Structure

1N0W is a Protein complex structure of sequences from [1] and Homo sapiens with MG, CL and EDO as ligands. Full crystallographic information is available from OCA.

Reference

Insights into DNA recombination from the structure of a RAD51-BRCA2 complex., Pellegrini L, Yu DS, Lo T, Anand S, Lee M, Blundell TL, Venkitaraman AR, Nature. 2002 Nov 21;420(6913):287-93. Epub 2002 Nov 10. PMID:12442171 [[Category: ]]

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