The Assembly and Intermolecular Properties of the hsp70-Hop-hsp90 Molecular Chaperone Complex
نویسندگان
چکیده
منابع مشابه
The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex.
The highly coordinated interactions of several molecular chaperones, including hsp70 and hsp90, are required for the folding and conformational regulation of a variety of proteins in eukaryotic cells, such as steroid hormone receptors and many other signal transduction regulators. The protein called Hop serves as an adaptor protein for hsp70 and hsp90 and is thought to optimize their functional...
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Hsp90 is an essential molecular chaperone required for the folding and activation of many hundreds of cellular "client" proteins. The ATP-dependent chaperone cycle involves significant conformational rearrangements of the Hsp90 dimer and interaction with a network of cochaperone proteins. Little is known about the mechanism of client protein binding or how cochaperone interactions modulate Hsp9...
متن کاملHop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery.
Hop, an abundant and conserved protein of unresolved function, binds concomitantly with heat shock protein 70 (Hsp70) and Hsp90, participates with heat shock proteins at an intermediate stage of progesterone receptor assembly, and is required for efficient assembly of mature receptor complexes in vitro. A largely untested hypothesis is that Hop functions as an adaptor that targets Hsp90- to Hsp...
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The de novo biosynthesis of purines is carried out by a highly conserved metabolic pathway that includes several validated targets for anticancer, immunosuppressant, and anti-inflammatory chemotherapeutics. The six enzymes in humans that catalyze the 10 chemical steps from phosphoribosylpyrophosphate to inosine monophosphate were recently shown to associate into a dynamic multiprotein complex c...
متن کاملAn Hsp70/Hsp90 Co-Chaperone That Functions Within and Beyond Hsp70/Hsp90 Protein Folding Pathways
Molecular chaperones and their co-chaperones are crucial for the facilitation of efficient protein folding, and prevention of denaturation and aggregation of nascent polypeptides. Hsp70/Hsp90 organizing protein (Hop), a co-chaperone of the two major molecular chaperones, heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90), facilitates their interaction by acting as an adaptor betwee...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m206566200