- Title
- Allosteric Modulation of Human Hsp90α Conformational Dynamics:
- Creator
- Penkler, David L, Atilgan, Canan, Tastan Bishop, Özlem
- Date
- 2018
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/162936
- Identifier
- vital:40998
- Identifier
- https://doi.org/10.1021/acs.jcim.7b00630
- Description
- Central to Hsp90’s biological function is its ability to interconvert between various conformational states. Drug targeting of Hsp90’s regulatory mechanisms, including its modulation by cochaperone association, presents as an attractive therapeutic strategy for Hsp90 associated pathologies. In this study, we utilized homology modeling techniques to calculate full-length structures of human Hsp90α in closed and partially open conformations and used these structures as a basis for several molecular dynamics based analyses aimed at elucidating allosteric mechanisms and modulation sites in human Hsp90α.
- Format
- 23 page, pdf
- Language
- English
- Relation
- Journal of Chemical Information and Modeling, Penkler, D.L., Atilgan, C. and Tastan Bishop, O., 2018. Allosteric Modulation of Human Hsp90α Conformational Dynamics. Journal of Chemical Information and Modeling, 58(2), pp.383-404, Journal of Chemical Information and Modeling volume 58 number 2 383 404 January 2018 1549-960X
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the ACS Publications Terms of Use Statement (https://0-www.acs.org.wam.seals.ac.za/content/acs/en/terms.html)
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Tastan Bishop, Ozlem (Prof)
RU Research Unit in Bioinformatics (RUBi)
RU Department of Biochemistry, Microbiology and Bioinformatics
SDG 03. Good Health and Well-Being
| Thumbnail | File | Description | Size | Format | |||
|---|---|---|---|---|---|---|---|
| View Details | SOURCE1 | Allosteric Modulation of Human Hsp90α Conformational Dynamic.pdf | 12 MB | Adobe Acrobat PDF | View Details |