Intermolecular Interactions

Protein Crystallography

Biological function requires the regulated assembly of macromolecules. Detailed three-dimensional images of macromolecular complexes are essential to understand the basis for specific assembly of the components of such complexes and to develop inhibitors to disrupt pathogenic assemblies. We primarily use X-ray crystallography (see figure of a Laue X-ray diffraction pattern) to determine the structures of protein molecules and the higher ordered complexes that they form. These structures provide important hypotheses for function, which we test by biochemical and biophysical approaches, and details required for docking of potential inhibitors.

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Structural Analysis of Assembly of Clinically Important Proteins

Our laboratory explores the structural basis by which intermolecular interactions regulate biological function. Our current research projects include a potential cancer target (CtBP), a transcription factor (IRF5) implicated in autoimmune disease, and a model system for investigating intersubunit communication with nanosecond time resolution. In all cases, the functional properties depend upon regulation of subunit assembly by binding of ligands or phosphorylation. In the first two cases, development of inhibitors that disrupt oligomerization may lead to therapeutic agents useful in cancer and autoimmune disease.

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