Towards an Atomic Understanding of Double-Strand Break Repair: Crystal Structure of Human RAD52 Protein
Abstract
Defects in recombination-based DNA repair lead to human breast cancer and familial degenerative diseases. The RAD52 epistasis gene products, especially the human RAD52 protein plays important role in double-strand break (DSB) repair. The focus of this work is to further understanding of the molecular basis of DSBs by solving the three-dimensional structure of hRAD52 and this will contribute a detailed understanding of the molecular mechanisms of breast cancer. The hRAD52 forms ring structure in solution and multiple level of aggregation of rings. We studied its multiple levels of self-association and stability using dynamic light scattering (DLS) and differential scanning calorimetry (DSC). To investigate the basis for the extreme stability of RAD52 that was discovered, two mutants were also studied, RAD52 (1-192) and RAD52.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2002
- Accession Number
- ADA408102
Entities
People
- Gloria Borgstahl
- Wasantha K. Ranatunga
Organizations
- University of Toledo