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Literature summary for 3.4.23.16 extracted from

  • Wallqvist, A.; Smythers, G.W.; Covell, D.G.
    A cooperative folding unit in HIV-1 protease. Implications for protein stability and occurrence of drug-induced mutations (1998), Protein Eng., 11, 999-1005.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information observed enzyme mutations of HIV-1 protease, either naturally occuring or induced by drug therapy, are found in regions that are not structurally designed to withstand unfolding. These mutations are especially likely to occur in the flap region, a part of the protein which is not essentiall for stability of the protein, but does contribute significantly to the stability of the protease-drug complexes Human immunodeficiency virus 1

General Stability

General Stability Organism
observed enzyme mutations of HIV-1 protease, either naturally occuring or induced by drug therapy, are found in regions that are not structurally designed to withstand unfolding. These mutations are especially likely to occur in the flap region, a part of the protein which is not essential for stability of the protein, but does contribute significantly to the stability of the protease-drug complexes Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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