Redesign of the PAK1 autoinhibitory domain for enhanced stability and affinity in biosensor applications.

@article{Jha2011RedesignOT,
  title={Redesign of the PAK1 autoinhibitory domain for enhanced stability and affinity in biosensor applications.},
  author={Ramesh K Jha and Yi I. Wu and Jon S. Zawistowski and Chris MacNevin and Klaus Michael Hahn and Brian Kuhlman},
  journal={Journal of molecular biology},
  year={2011},
  volume={413 2},
  pages={513-22}
}
The inhibitory switch (IS) domain of p21-activated kinase 1 (PAK1) stabilizes full-length PAK1 in an inactive conformation by binding to the PAK1 kinase domain. Competitive binding of small guanosine triphosphatases to the IS domain disrupts the autoinhibitory interactions and exposes the IS domain binding site on the surface of the kinase domain. To build an affinity reagent that selectively binds the activated state of PAK1, we used molecular modeling to reengineer the isolated IS domain so… CONTINUE READING

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