Sandbox Reserved 712: Difference between revisions
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3ggu is a drug resistant HIV protease. Shown is a patient's variant in complex with darunavir. | 3ggu is a drug resistant HIV protease. Shown is a patient's variant in complex with darunavir. | ||
HIV proteases(PR) are essential for the functioning of the retrovirus that causes AIDS. HIV needs active proteases to process Gag & Gap - Polymerase polyprotein precursors into mature structural proteins and replicative enzymes. | HIV proteases (PR) are essential for the functioning of the retrovirus that causes AIDS. HIV needs active proteases to process Gag & Gap - Polymerase polyprotein precursors into mature structural proteins and replicative enzymes. | ||
HIV proteases contain a highly conserved region Asp - Thr - Gly (Asp25, Thr26 and Gly27), with the aspartic residue beeing the active site in the aspartyl protease.[[(1)]] | HIV proteases contain a highly conserved region Asp - Thr - Gly (Asp25, Thr26 and Gly27), with the aspartic residue beeing the active site in the aspartyl protease.[[(1)]] | ||
Because of its importance for the life-cycle of the retrovirus, HIV-PR are the major target for | |||
HIV protease inhibitors are the most potent agens used in anti-HIV treatment. However it occurs that HIV PR develops a resistance to the inhibitor. [[(2)]] | Because of its importance for the life-cycle of the retrovirus, HIV-PR are the major target for anti-HIV treatment. | ||
HIV protease inhibitors are the most potent agens used in anti-HIV treatment. However it occurs that HIV-PR develops a resistance to the inhibitor. [[(2)]] | |||
== '''Activity''' == | == '''Activity''' == | ||
Revision as of 12:35, 27 December 2012
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Description
3ggu is a drug resistant HIV protease. Shown is a patient's variant in complex with darunavir.
HIV proteases (PR) are essential for the functioning of the retrovirus that causes AIDS. HIV needs active proteases to process Gag & Gap - Polymerase polyprotein precursors into mature structural proteins and replicative enzymes.
HIV proteases contain a highly conserved region Asp - Thr - Gly (Asp25, Thr26 and Gly27), with the aspartic residue beeing the active site in the aspartyl protease.(1)
Because of its importance for the life-cycle of the retrovirus, HIV-PR are the major target for anti-HIV treatment. HIV protease inhibitors are the most potent agens used in anti-HIV treatment. However it occurs that HIV-PR develops a resistance to the inhibitor. (2)
Activity
Structure
Applications
External Resources
References
(1) Kohl, N. E., E. A. Emini, W. A. Schleif, L. J. Davis, J. C. Heimbach, R. A. F. Dixon, E. M. Scolnick, and I. S. Sigal. 1988. Active human immunodeficiency virus protease is required for viral infectivity. Proc. Natl. Acad. Sci. USA 85:4686-4690.
(2) Watkins T, Resch W, Irlbeck D, Swanstrom R (February 2003). "Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors". Antimicrob. Agents Chemother. 47 (2): 759–69. doi:10.1128/AAC.47.2.759-769.2003. PMC 151730. PMID 12543689.
Contributors
Julia Baaske, Angelika Wackerl
