Predicting Allosteric Effects from Orthosteric Binding in Hsp90-Ligand Interactions: Implications for Fragment-Based Drug Design

Keyphrases

• Orthosteric 100%
• Heat Shock Protein 90 (Hsp90) 100%
• Allosteric Effect 100%
• Hydrogen-deuterium Exchange Mass Spectrometry 100%
• Fragment Based Drug Design 100%
• Low Affinity 50%
• High Affinity 50%
• Affinity Ligands 50%
• Binding Site 33%
• Conformational Change 33%
• Orthosteric Site 33%
• Protein-ligand Interaction 33%
• Allostery 33%
• Highly Sensitive 16%
• Structural Insights 16%
• Dissociation Constant 16%
• Structural Information 16%
• Amides 16%
• Structural Dynamics 16%
• High-throughput Methods 16%
• Dynamic Information 16%
• Protein Dynamics 16%
• ATPase Domain 16%
• Natural Inhibitors 16%
• Ligand Dissociation 16%
• Protein-ligand Complex 16%

Biochemistry, Genetics and Molecular Biology

• Allosteric Regulation 100%
• Hsp90 100%
• Hydrogen/Deuterium Exchange Mass Spectrometry 100%
• Dynamics 50%
• Binding Site 33%
• Conformational Change 33%
• Protein-Ligand Interaction 33%
• ATPase 16%
• Dissociation Constant 16%
• N-Terminus 16%
• Protein Ligand 16%
• Protein Dynamics 16%