Determinants of protein–protein recognition by four helix bundles: changing the dimerization specificity of Tet repressor

@article{Schnappinger1998DeterminantsOP,
  title={Determinants of protein–protein recognition by four helix bundles: changing the dimerization specificity of Tet repressor},
  author={D. Schnappinger and P. Schubert and K. Pfleiderer and W. Hillen},
  journal={The EMBO Journal},
  year={1998},
  volume={17}
}
  • D. Schnappinger, P. Schubert, +1 author W. Hillen
  • Published 1998
  • Medicine, Biology
  • The EMBO Journal
  • Homo‐ and heterodimerization is essential for the activity of many proteins, particularly transcription factors. One widely distributed structural motif for protein recognition is the four helix bundle. To understand the molecular details determining specificity of subunit recognition in a dimer formed by a four helix bundle, we investigated Tet repressor (TetR) sequence variants TetR(B) and TetR(D), which do not form heterodimers. We used molecular modeling to identify residues with the… CONTINUE READING
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