Synthesis and Evaluation of a Novel Deguelin Derivative, L80, which Disrupts ATP Binding to the C-terminal Domain of Heat Shock Protein 90

2015 ◽  
Vol 88 (2) ◽  
pp. 245-255 ◽  
Author(s):  
Su-Chan Lee ◽  
Hye-Young Min ◽  
Hoon Choi ◽  
Ho Shin Kim ◽  
Kyong-Cheol Kim ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Atp Binding ◽  
Terminal Domain

scholarly journals The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

1997 ◽  
Vol 272 (38) ◽  
pp. 23843-23850 ◽  
Author(s):  
James P. Grenert ◽  
William P. Sullivan ◽  
Patrick Fadden ◽  
Timothy A. J. Haystead ◽  
Jenny Clark ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Amino Terminal Domain

scholarly journals Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

2000 ◽  
Vol 97 (23) ◽  
pp. 12524-12529 ◽  
Author(s):  
A. Chadli ◽  
I. Bouhouche ◽  
W. Sullivan ◽  
B. Stensgard ◽  
N. McMahon ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Heat Shock Protein 90 ◽  
Terminal Domain

scholarly journals Functional characterization of heat-shock protein 90 fromOryza sativaand crystal structure of its N-terminal domain

2015 ◽  
Vol 71 (6) ◽  
pp. 688-696 ◽  
Author(s):  
Swetha Raman ◽  
Kaza Suguna
Keyword(s):  
Crystal Structure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Biochemical Characterization ◽  
Functional Characterization ◽  
Cell Signalling ◽  
Physiological Role ◽  
Heat Shock Protein 90 ◽  
Terminal Domain

Heat-shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is essential for the normal functioning of eukaryotic cells. It plays crucial roles in cell signalling, cell-cycle control and in maintaining proteome integrity and protein homeostasis. In plants, Hsp90s are required for normal plant growth and development. Hsp90s are observed to be upregulated in response to various abiotic and biotic stresses and are also involved in immune responses in plants. Although there are several studies elucidating the physiological role of Hsp90s in plants, their molecular mechanism of action is still unclear. In this study, biochemical characterization of an Hsp90 protein from rice (Oryza sativa; OsHsp90) has been performed and the crystal structure of its N-terminal domain (OsHsp90-NTD) was determined. The binding of OsHsp90 to its substrate ATP and the inhibitor 17-AAG was studied by fluorescence spectroscopy. The protein also exhibited a weak ATPase activity. The crystal structure of OsHsp90-NTD was solved in complex with the nonhydrolyzable ATP analogue AMPPCP at 3.1 Å resolution. The domain was crystallized by cross-seeding with crystals of the N-terminal domain of Hsp90 fromDictyostelium discoideum, which shares 70% sequence identity with OsHsp90-NTD. This is the second reported structure of a domain of Hsp90 from a plant source.

scholarly journals The Heat Shock Protein 90 Antagonist Novobiocin Interacts with a Previously Unrecognized ATP-binding Domain in the Carboxyl Terminus of the Chaperone

2000 ◽  
Vol 275 (47) ◽  
pp. 37181-37186 ◽  
Author(s):  
Monica G. Marcu ◽  
Ahmed Chadli ◽  
Ilham Bouhouche ◽  
Maria Catelli ◽  
Leonard M. Neckers
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Binding Domain ◽  
Carboxyl Terminus ◽  
Atp Binding

New dihydropyrimidin-2(1H)-one based Hsp90 C-terminal inhibitors

RSC Advances ◽  
2016 ◽  
Vol 6 (85) ◽  
pp. 82330-82340 ◽  
Author(s):  
S. Terracciano ◽  
A. Foglia ◽  
M. G. Chini ◽  
M. C. Vaccaro ◽  
A. Russo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Cancer Therapy ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
New Class ◽  
Terminal Domain ◽  
Novel Strategy

The inhibition of the C-terminal domain of heat shock protein 90 (Hsp90) is emerging as a novel strategy for cancer therapy, therefore the identification of a new class of C-terminal inhibitors is strongly required.

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