Structure of a BRCA1/BARD1 Complex: a Heterodimeric RING-RING Interaction
The N-terminal 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 N-terminal RING domain heterodimer of BRCA1 and BARD1. Comparison with the RAG1 RING homodimer 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 provdes a framework for understanding cancer-causing mutations at the molecular level.
- Research Organization:
- Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 15007892
- Report Number(s):
- PNNL-SA-34960; 2034; 1933; KP1704020; TRN: US200423%%95
- Journal Information:
- Nature Structural Biology, 8(10):833-837, Vol. 8, Issue 10
- Country of Publication:
- United States
- Language:
- English
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