Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants.

Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants.

The two cytosolic/nuclear isoforms of the molecular chaperone HSP90, stress-inducible HSP90α and constitutively expressed HSP90β, fold, assemble and maintain the three-dimensional structure of numerous client proteins. Because many HSP90 clients are important in cancer, several HSP90 inhibitors have...

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Main Authors: Thomas L Prince, Toshiki Kijima, Manabu Tatokoro, Sunmin Lee, Shinji Tsutsumi, Kendrick Yim, Candy Rivas, Sylvia Alarcon, Harvey Schwartz, Kofi Khamit-Kush, Bradley T Scroggins, Kristin Beebe, Jane B Trepel, Len Neckers
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0141786&type=printable
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