Article
The region adjacent to the highly immunogenic site and shielded by the middle domain is responsible for self-oligomerization/client binding of the HSP90 molecular chaperone.
Biochemistry - 15 Jun 2004
Nemoto Takayuki K, Fukuma Yutaka, Yamada Shin-ichi, Kobayakawa Takeshi, Ono Toshio, Ohara-Nemoto Yuko
Abstract excerpt
We here investigated the mechanism of self-oligomerization of the 90-kDa heat shock protein (HSP90) molecular chaperone, because it is known that this oligomerization reflects the client-binding activity. The transition temperatures for the self-oligomerization of the full-length forms of human HSP90alpha and HtpG (bacterial HSP90), i.e., 45 and 60 degrees C, respectively, were identical to those for the...
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