Hijacking Molecular Plasticity to Fine Tune Nuclear Receptor Signaling: Chemical Biology and Precision Therapeutics

This webinar will highlight a new platform for structure-function analysis to dissect activation mechanisms of nuclear receptors (NRs).

Regulation of gene programs controlled by NRs is driven in part by alterations in the conformational ensemble of the receptor upon ligand binding. Dr. Patrick Griffin will describe the development of a structural proteomics platform that includes differential hydrogen/deuterium exchange (HDX), cross-linking mass spectrometry (XL-MS), co-crystallography and SAXS to structure-function studies.

This platform was used to build an integrative structural model for activation of the nuclear receptor RORG (ROR-gamma), a key lineage defining transcription factor in Th17 cells. Results will be presented from chemo-proteomic and structural proteomic studies that investigate the impact of ligand binding on coregulatory engagement and that examine how RORG recognizes sequence specific DNA response elements.

You will learn

• How mass spectrometry can answer structural biology questions
• What mass spectrometry techniques are useful for structural proteomics
• What it takes to build a structural proteomics platform
  

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