Functional Mechanism of the Molecular Chaperone GroE
نویسندگان
چکیده
منابع مشابه
Review: a structural view of the GroE chaperone cycle.
The GroE chaperone system consists of two ring-shaped oligomeric components whose association creates different functional states. The most remarkable property of the GroE system is the ability to fold proteins under conditions where spontaneous folding cannot occur. To achieve this, a fully functional system consisting of GroEL, the cochaperone GroES, and ATP is necessary. Driven by ATP bindin...
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A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90.
The 90-kDa heat shock protein (HSP90) acts as a specific molecular chaperone in the folding and regulates a wide range of associated proteins such as steroid hormone receptors. It is known that HSP90 possesses two different chaperone sites, both in the N- and C-domains, and that the chaperone activity of HSP90 is blocked by binding of geldanamycin (GA) to the N-domain, the same as the ATP-bindi...
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ژورنال
عنوان ژورنال: Nippon Nōgeikagaku Kaishi
سال: 1996
ISSN: 0002-1407,1883-6844
DOI: 10.1271/nogeikagaku1924.70.576