Article
Drug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH.
Protein science : a publication of the Protein Society - 1 Aug 1999
Xie D, Gulnik S, Gustchina E, Yu B, Shao W, Qoronfleh W, Nathan A, Erickson J W
Abstract excerpt
The monomer-dimer equilibrium for the human immunodeficiency virus type 1 (HIV-1) protease has been investigated under physiological conditions. Dimer dissociation at pH 7.0 was correlated with a loss in beta-sheet structure and a lower degree of ANS binding. An autolysis-resistant mutant, Q7K/L33I/L63I, was used to facilitate sedimentation equilibrium studies at neutral pH where the wild-type enzyme is typically...
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