PPARγ non-covalent antagonists exhibit mutable binding modes with a similar free energy of binding: a case study
Author:
Affiliation:
1. Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Block 105, 1113 Sofia, Bulgaria
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2016.1151830
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1. Dynamics of Nuclear Receptor Helix-12 Switch of Transcription Activation by Modeling Time-Resolved Fluorescence Anisotropy Decays
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3. Partial Agonists Activate PPARγ Using a Helix 12 Independent Mechanism
4. Structure of the intact PPAR-γ–RXR-α nuclear receptor complex on DNA
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