We present the first NMR study of the interaction between heat shock protein 90 (Hsp90) and amino (N)-terminal inhibitors 17-AAG, and AUY922, and carboxy (C)-terminal modulators SM253, and LB51. We show that the two ATP mimics, 17-AAG and AUY922, bind deeply within the ATP binding pocket of the N-terminal domain, consistent with the crystal structures. In contrast, SM253, a C-terminal Hsp90 modulator, binds to the linker region between the N and middle domains. We also show that C-terminal...
[ASAP] Optimizing the First TPR Domain of the Human SPAG1 Protein Provides Insight into the HSP70 and HSP90 Binding Properties
Optimizing the First TPR Domain of the Human SPAG1 Protein Provides Insight into the HSP70 and HSP90 Binding Properties
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00052/20210319/images/medium/bi1c00052_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00052
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03-20-2021 02:31 AM
[NMR paper] Nucleotide Binding and Active Site Gate Dynamics for the Hsp90 Chaperone ATPase Domain from Benchtop and High Field 19F NMR Spectroscopy.
Nucleotide Binding and Active Site Gate Dynamics for the Hsp90 Chaperone ATPase Domain from Benchtop and High Field 19F NMR Spectroscopy.
Related Articles Nucleotide Binding and Active Site Gate Dynamics for the Hsp90 Chaperone ATPase Domain from Benchtop and High Field 19F NMR Spectroscopy.
J Phys Chem B. 2020 Mar 25;:
Authors: Rashid S, Lee BL, Wajda B, Spyracopoulos L
Abstract
Protein turnover in cells is regulated by the ATP dependent activity of the Hsp90 chaperone. In concert with accessory proteins, ATP hydrolysis drives...
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03-29-2020 12:14 PM
[NMR paper] NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine.
NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine.
Related Articles NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine.
J Biomol NMR. 2017 Jun 26;:
Authors: Pederson K, Chalmers GR, Gao Q, Elnatan D, Ramelot TA, Ma LC, Montelione GT, Kennedy MA, Agard DA, Prestegard JH
Abstract
A strategy for acquiring structural information from sparsely isotopically labeled large proteins is illustrated with an application to the E. coli heat-shock...
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06-28-2017 07:37 PM
NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13 C-methyl alanine
NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13 C-methyl alanine
Abstract
A strategy for acquiring structural information from sparsely isotopically labeled large proteins is illustrated with an application to the E. coli heat-shock protein, HtpG (high temperature protein G), a 145Â*kDa dimer. It uses 13C-alanine methyl labeling in a perdeuterated background to take advantage of the sensitivity and resolution of Methyl-TROSY spectra, as well as the backbone-centered structural information from 1Hâ??13C residual dipolar...
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06-27-2017 03:27 AM
[NMR paper] Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry and NMR.
Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry and NMR.
J Phys Chem B. 2016 Aug 29;
Authors: Toleikis Z, Sirotkin VA, Skvarnavi?ius G, Smirnovien? J, Roumestand C, Matulis D, Petrauskas V
Abstract
Human heat shock protein 90 (Hsp90) is a key...
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08-31-2016 02:34 PM
Specific Binding of Tetratricopeptide Repeat Proteinsto Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90)Is Regulated by Affinity and Phosphorylation
Specific Binding of Tetratricopeptide Repeat Proteinsto Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90)Is Regulated by Affinity and Phosphorylation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00801/20151125/images/medium/bi-2015-00801d_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00801
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11-26-2015 12:22 PM
[NMR paper] A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.
A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.
J Med Chem. 2013 Jan 30;
Authors: Dal Piaz F, Vassallo A, Temraz A, Cotugno R, Belisario MA, Bifulco G, Chini MG, Pisano C, De Tommasi N, Braca A
Abstract
The potential of Heat Shock Protein 90 (Hsp90) as a therapeutic target...
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02-03-2013 10:19 AM
[NMR paper] NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding
NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
Related Articles NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
Chembiochem. 2003 Sep 5;4(9):870-7
Authors: Dehner A, Furrer J, Richter K, Schuster I, Buchner J, Kessler H
Hsp90 is one of the most abundant chaperone proteins in the cytosol. In an ATP-dependent manner it plays an essential role in the folding and activation of a...
Using NMR to identify binding regions for N and C-terminal Hsp90 inhibitors using Hsp90 domains
Linear Mode
