1jm7
Solution structure of the BRCA1/BARD1 RING-domain heterodimer
|
OverviewOverview
The RING domain of the breast and ovarian cancer tumor suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mutations found within this domain. We present the solution structure of the heterodimer formed between the RING domains of BRCA1 and BARD1. Comparison with the RING homodimer of the V(D)J recombination-activating protein RAG1 reveals the structural diversity of complexes formed by interactions between different RING domains. The BRCA1-BARD1 structure provides a model for its ubiquitin ligase activity, illustrates how the BRCA1 RING domain can be involved in associations with multiple protein partners and provides a framework for understanding cancer-causing mutations at the molecular level.
DiseaseDisease
Known diseases associated with this structure: Breast cancer, susceptibility to OMIM:[601593], Breast cancer-1 OMIM:[113705], Breast-ovarian cancer OMIM:[113705], Ovarian cancer OMIM:[113705], Papillary serous carcinoma of the peritoneum OMIM:[113705]
About this StructureAbout this Structure
1JM7 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex., Brzovic PS, Rajagopal P, Hoyt DW, King MC, Klevit RE, Nat Struct Biol. 2001 Oct;8(10):833-7. PMID:11573085
Page seeded by OCA on Thu Feb 21 13:24:17 2008