Macromolecular inhibitors of HIV-1 protease. Characterization of designed heterodimers.

@article{Rozzelle2000MacromolecularIO,
  title={Macromolecular inhibitors of HIV-1 protease. Characterization of designed heterodimers.},
  author={James Rozzelle and Deborah S Dauber and Stephen Todd and Richard. L. Kelley and Charles S. Craik},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 10},
  pages={7080-6}
}
Defective variants of human immunodeficiency virus type 1 (HIV-1) protease (HIV PR) have been engineered to inhibit wild-type (wt) HIV PR activity. These variants were designed to promote the formation of heterodimers and to destabilize the formation of inactive variant homodimers of HIV-1 protease through substitutions at Asp-25, Ile-49, and Gly-50 (Babé, L. M., Rosé, J., and Craik, C. S. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 10069-10073; McPhee, F., Good, A. C., Kuntz, I. D., and Craik… CONTINUE READING

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