Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions.

@article{Peng2000ReconstitutionOT,
  title={Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions.},
  author={Hongzhuang Peng and Gillian E Begg and David C. Schultz and Jonathan R. Friedman and David E. Jensen and David W. Speicher and F. Rauscher},
  journal={Journal of molecular biology},
  year={2000},
  volume={295 5},
  pages={1139-62}
}
The KRAB domain is a 75 amino acid residue transcriptional repression module commonly found in eukaryotic zinc-finger proteins. KRAB-mediated gene silencing requires binding to the corepressor KAP-1. The KRAB:KAP-1 interaction requires the RING-B box-coiled coil (RBCC) domain of KAP-1, which is a widely distributed motif, hypothesized to be a protein-protein interface. Little is known about RBCC-mediated ligand binding and the role of the individual sub-domains in recognition and specificity… CONTINUE READING

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