Drug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH.

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/...

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Detalhes bibliográficos
Main Authors: Xie, D., Gulnik, S., Gustchina, E., Yu, B., Shao, W., Qoronfleh, W., Nathan, A., Erickson, J. W.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 1999
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144419/
https://ncbi.nlm.nih.gov/pubmed/10452615
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