- Title
- Modulation of human Hsp90α conformational dynamics by allosteric ligand interaction at the c-terminal domain:
- Creator
- Penkler, David L, Tastan Bishop, Özlem
- Date
- 2018
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/148402
- Identifier
- vital:38736
- Identifier
- DOI: 10.1101/386755
- Description
- Recent years have seen heat shock protein 90 kDa (Hsp90) attract significant interest as a viable drug target, particularly for cancer. To date, designed inhibitors that target the ATPase domain demonstrate potent anti-proliferative effects, but have failed clinical trials due to high levels of associated toxicity. To circumvent this, the focus has shifted away from the ATPase domain. One option involves modulation of the protein through allosteric activation/inhibition. Here, we propose a novel approach: we use previously obtained information via residue perturbation scanning coupled with dynamic residue network analysis to identify allosteric drug targeting sites for inhibitor docking.
- Format
- Language
- English
- Relation
- Scientific reports, Penkler, D.L. and Bishop, Ö.T., 2019. Modulation of human Hsp90α conformational dynamics by allosteric ligand interaction at the c-terminal domain. Scientific reports, 9(1), pp.1-17., Scientific reports volume 9 number 1 1 17 2018 2045-2322
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the nature research Terms and Conditions statement (https://0-www.nature.com.wam.seals.ac.za/info/terms-and-conditions)
- Hits: 450
- Visitors: 556
- Downloads: 114
Collections
Tastan Bishop, Ozlem (Prof)
RU Research Unit in Bioinformatics (RUBi)
SDG 03. Good Health and Well-Being
RU Department of Biochemistry, Microbiology and Bioinformatics
| Thumbnail | File | Description | Size | Format | |||
|---|---|---|---|---|---|---|---|
| View Details | SOURCE1 | Modulation of human Hsp90α conformational dynamics.pdf | 4 MB | Adobe Acrobat PDF | View Details |