Mutations in BRCA1/BARD1 RING-domain heterodimer: Difference between revisions
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*<scene name='75/751104/L22s/3'>Mutation L22S: </scene> <jmol><jmolLink><script>animation off; frame 1</script><text>Wild type</text></jmolLink></jmol> and the <jmol><jmolLink><script>animation off; frame 2</script><text>Mutation</text></jmolLink></jmol>. <jmol><jmolLink><script>animation off; frame all</script><text>Mutated and wildtype residues together</text></jmolLink></jmol>. Click here to see an <jmol><jmolLink><script>animation on; animation mode loop; frame play</script><text>animation</text></jmolLink></jmol> of both states. Putative new hydrogen bonds were added. | *<scene name='75/751104/L22s/3'>Mutation L22S: </scene> <jmol><jmolLink><script>animation off; frame 1</script><text>Wild type</text></jmolLink></jmol> and the <jmol><jmolLink><script>animation off; frame 2</script><text>Mutation</text></jmolLink></jmol>. <jmol><jmolLink><script>animation off; frame all</script><text>Mutated and wildtype residues together</text></jmolLink></jmol>. Click here to see an <jmol><jmolLink><script>animation on; animation mode loop; frame play</script><text>animation</text></jmolLink></jmol> of both states. Putative new hydrogen bonds were added. <scene name='75/751104/L22s/6'>TextToBeDisplayed</scene> | ||
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Revision as of 13:30, 14 February 2017
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.[1] . Pathogenic mutations are shown in magenta, benign mutations are shown in green. Pathogenic mutations
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Benign mutations
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References
- ↑ Brzovic PS, Rajagopal P, Hoyt DW, King MC, Klevit RE. Structure of a BRCA1-BARD1 heterodimeric RING-RING complex. Nat Struct Biol. 2001 Oct;8(10):833-7. PMID:11573085 doi:10.1038/nsb1001-833