Proteus in the world of proteins: conformational changes in protein kinases.

  title={Proteus in the world of proteins: conformational changes in protein kinases.},
  author={Matthias Rabiller and Matthaeus Getlik and Sabine Kl{\"u}ter and Andr{\'e} Richters and Sandra T{\"u}ckmantel and Jeffrey R. Simard and Daniel Rauh},
  journal={Archiv der Pharmazie},
  volume={343 4},
The 512 protein kinases encoded by the human genome are a prime example of nature's ability to create diversity by introducing variations to a highly conserved theme. The activity of each kinase domain is controlled by layers of regulatory mechanisms involving different combinations of post-translational modifications, intramolecular contacts, and intermolecular interactions. Ultimately, they all achieve their effect by favoring particular conformations that promote or prevent the kinase domain… CONTINUE READING

From This Paper

Topics from this paper.


Publications citing this paper.
Showing 1-10 of 16 extracted citations

Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences • 2012

Similar Papers

Loading similar papers…