Mutations Proximal to Sites of Autoproteolysis and the α‑Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV‑1 Protease

N-Terminal self-cleavage (autoprocessing) of the HIV-1 protease precursor is crucial for liberating the active dimer. Under drug pressure, evolving mutations are predicted to modulate autoprocessing, and the reduced catalytic activity of the mature protease (PR) is likely compensated by enhanced con...

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Veröffentlicht in:	Biochemistry (Easton) 2015-09, Vol.54 (35), p.5414-5424
Hauptverfasser:	Louis, John M, Deshmukh, Lalit, Sayer, Jane M, Aniana, Annie, Clore, G. Marius
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites - physiology Drug Resistance, Multiple - physiology HIV Protease - genetics HIV Protease - metabolism Molecular Sequence Data Mutation - genetics Protein Structure, Secondary Proteolysis
Online-Zugang:	Volltext
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