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TitleStructure of a BRCA1-BARD1 heterodimeric RING-RING complex.
Journal, issue, pagesNat Struct Biol, Vol. 8, Issue 10, Page 833-837, Year 2001
Publish dateOct 18, 2001
AuthorsP S Brzovic / P Rajagopal / D W Hoyt / M C King / R E Klevit /
PubMed AbstractThe 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 ...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.
External linksNat Struct Biol / PubMed:11573085
MethodsNMR (solution)
Structure data

PDB-1jm7:
Solution structure of the BRCA1/BARD1 RING-domain heterodimer
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsANTITUMOR / BRCA1 / BARD1 / RING finger / zinc-binding protein / heterodimer / ubiquitin ligase

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