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• W1987643357 abstract "Electron microscopy using the low-angle rotary shadowing replica method showed that the HSP90 dimer consists of four globular domains aligning in a tandem fashion. When decorated with two monoclonal antibodies against epitopes mapped on the N-terminal region of HSP90, these antibodies bound to both ends of the HSP90 dimer. A C-terminal region specific antibody was shown to bind to the side of HSP90. These results support a model for HSP90 dimer whereby two HSP90 monomers are arranged in an antiparallel fashion and dimerize through the C-terminal domain. Treatment of HSP90 at elevated temperatures or with ATP at room temperature, though not with ADP, induces molecular transformation of the linear HSP90 dimer into an O-ring-shaped structure." @default.
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• W1987643357 date "1999-01-01" @default.
• W1987643357 modified "2023-10-11" @default.
• W1987643357 title "Monomer Arrangement in HSP90 Dimer as Determined by Decoration with N and C-Terminal Region Specific Antibodies" @default.
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• W1987643357 doi "https://doi.org/10.1006/jmbi.1998.2349" @default.
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