Targeting structural flexibility in HIV-1 protease inhibitor binding.

@article{Hornak2007TargetingSF,
  title={Targeting structural flexibility in HIV-1 protease inhibitor binding.},
  author={Viktor Hornak and Carlos Simmerling},
  journal={Drug discovery today},
  year={2007},
  volume={12 3-4},
  pages={
          132-8
        }
}
HIV-1 protease remains an important anti-AIDS drug target. Although it has been known that ligand binding induces large conformational changes in the protease, the dynamic aspects of binding have been largely ignored. Several computational models describing protease dynamics have been reported recently. These have reproduced experimental observations, and have also explained how ligands gain access to the binding site through dynamic behavior of the protease. Specifically, the transitions… CONTINUE READING

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VIEW 2 EXCERPTS
CITES BACKGROUND & METHODS
HIGHLY INFLUENCED

References

Publications referenced by this paper.
SHOWING 1-10 OF 63 REFERENCES

Drug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations.

  • Protein science : a publication of the Protein Society
  • 2002
VIEW 7 EXCERPTS
HIGHLY INFLUENTIAL

b-lactam compounds as apparently uncompetitive inhibitors of HIV-1 protease

T Sperka
  • Bioorg. Med. Chem. Lett
  • 2005
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune-deficiency syndrome

F Barresinoussi
  • (AIDS). Science
  • 1983
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

Flap opening mechanism of HIV-1 protease.

  • Journal of molecular graphics & modelling
  • 2006

HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2006
VIEW 2 EXCERPTS