Human heat shock protein 90 (Hsp90) is one of the most important chaperones that play a role in the late stages of protein folding. Errors in the process of the chaperone cycle can lead to diseases such as cancer and neurodegenerative diseases. Therefore, the activity of Hsp90 must be carefully regulated. One of the possibilities is allosteric regulation by its natural allosteric modulators-nucleotides, co-chaperones and client proteins-and synthetic small-molecule allosteric modulators, such as...
[NMR paper] Insights into the stabilization of interferon alpha by two surfactants revealed by STD-NMR spectroscopy
Insights into the stabilization of interferon alpha by two surfactants revealed by STD-NMR spectroscopy
Surfactants are commonly used in biopharmaceutical formulations to stabilize proteins against aggregation. However, the choice of a suitable surfactant for a particular protein is decided mostly empirically, and their mechanism of action on molecular level is largely unknown. Here we show that a straightforward label-free method, saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy, can be used to detect protein-surfactant interactions in formulations of a...
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10-20-2022 06:37 PM
[NMR paper] Using NMR to identify binding regions for N and C-terminal Hsp90 inhibitors using Hsp90 domains
Using NMR to identify binding regions for N and C-terminal Hsp90 inhibitors using Hsp90 domains
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...
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04-27-2021 10:40 AM
[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
http://feeds.feedburner.com/~r/acs/bichaw/~4/erk3hPL4q-U
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Insights into the Allosteric Regulation of Human Hsp90 Revealed by NMR Spectroscopy
Linear Mode
