Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex.

@article{Brzovic2003BindingAR,
  title={Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex.},
  author={Peter S. Brzovic and Jennifer R. Keeffe and Hiroyuki Nishikawa and Keiko Miyamoto and David L Fox and Mamoru Fukuda and Tomohiko Ohta and Rachel E. Klevit},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 10},
  pages={5646-51}
}
BRCA1 is a breast and ovarian cancer tumor suppressor protein that associates with BARD1 to form a RINGRING heterodimer. The BRCA1BARD1 RING complex functions as an ubiquitin (Ub) ligase with activity substantially greater than individual BRCA1 or BARD1 subunits. By using NMR spectroscopy and site-directed mutagenesis, we have mapped the binding site on the BRCA1BARD1 heterodimer for the Ub-conjugating enzyme UbcH5c. The results demonstrate that UbcH5c binds only to the BRCA1 RING domain and… CONTINUE READING
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