Autoprocessing of HIV-1 protease is tightly coupled to protein folding

@article{Louis1999AutoprocessingOH,
  title={Autoprocessing of HIV-1 protease is tightly coupled to protein folding},
  author={J. Louis and G. Clore and A. Gronenborn},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={868-875}
}
In the Gag-Pol polyprotein of HIV-1, the 99-amino acid protease is flanked at its N-terminus by a transframe region (TFR) composed of the transframe octapeptide (TFP) and 48 amino acids of the p6pol, separated by a protease cleavage site. The intact precursor (TFP-p6pol-PR) has very low dimer stability relative to that of the mature enzyme and exhibits negligible levels of stable tertiary structure. Thus, the TFR functions by destabilizing the native structure, unlike proregions found in… Expand
Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions
Solution Structure of the Mature HIV-1 Protease Monomer
Folded Monomer of HIV-1 Protease*
Kinetic characterization of the critical step in HIV-1 protease maturation
Three-dimensional structure of a monomeric form of a retroviral protease.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 39 REFERENCES
Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.
A Transient Precursor of the HIV-1 Protease
...
1
2
3
4
...