Modulation of HIV-1 Protease Autoprocessing by Charge Properties of Histidine 69 Surface Residue.
Modulation of HIV-1 Protease Autoprocessing by Charge Properties of Histidine 69 Surface Residue. - Related Articles
Modulation of HIV-1 Protease Autoprocessing by Charge Properties of Histidine 69 Surface Residue.
J Virol. 2009 May 20;
Authors: Huang L, Sayer JM, Swinford M, Louis JM, Chen C
Mature, fully active HIV protease (PR) is liberated from the Gag-Pol precursor via regulated autoprocessing. A chimeric protease precursor, GST-TFR-PR-FLAG, also undergoes N-terminal autocatalytic maturation when expressed in E. coli. Mutation of the surface residue H69 to glutamic acid, but not to several neutral or basic amino acids, impedes protease autoprocessing in bacteria and mammalian cells. Only a fraction of the mature PRH69E folds into active enzymes, with an apparent Kd significantly higher than the wild type protease, corroborating the marked retardation of the in vitro N-terminal autocatalytic processing of the TFR-PRH69E, and suggesting a folding defect in the precursor.
PMID: 19457992 [PubMed - as supplied by publisher] [PubMed-HIV]
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