Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism.

@article{Leverson1998PointMI,
  title={Point mutations in v-Myb disrupt a cyclophilin-catalyzed negative regulatory mechanism.},
  author={Joel D. Leverson and Scott A Ness},
  journal={Molecular cell},
  year={1998},
  volume={1 2},
  pages={203-11}
}
The c-Myb protein is controlled by intramolecular interactions, and point mutations can enhance its oncogenic activity. We tested whether conformational changes regulate c-Myb and found that Cyp-40, a widely distributed cyclophilin and peptidyl-prolyl isomerase, could inhibit c-Myb DNA binding activity. Inhibition by Cyp-40 required both its C-terminal protein-interaction domain, which bound specifically to c-Myb, and its N-terminal catalytic domain and was blocked by the competitive inhibitor… CONTINUE READING