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J Mol Biol. 1999 Jan 22;285(3):903-7.

Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies.

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Department of Cell Biology, The Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, 113-8613, Japan.


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.

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