Crystallography of rhodopsin, cell adhesion proteins and enzymes

The focus in my group is on the application of X-ray crystallographic techniques to determine the three -dimensional structures of biologically interesting macromolecules. Understanding the arrangements of atoms in molecules is useful for asking questions about their chemistry and function.

We are interested in a range of proteins and collaborate extensively with investigators whose emphasis is on the chemistry and biology of the molecules. Here’s a partial list of structure determinations currently underway in my lab.

Rhodopsin. This G protein-coupled receptor is the photo-active molecule in the visual system. In response to light, it initiates a signaling cascade that results in signals being sent to the brain. We have solved the ground-state structure as well as a photo-activated form of the protein. We are also pursuing studies of rhodopsin in complex with its protein ligands. This work is being done in collaboration with Kris Palczewski at Case-Western Reserve University.

Streptavidin. Biotin binds very strongly to streptavidin, and we want to understand the intermolecular interactions involved. In collaboration with Pat Stayton (Univ. of Washington) and Terry Lybrand (Vanderbilt Univ.), we are applying biophysical, computational and crystallographic methods to understand how the protein recognizes its small molecule ligands

In addition to these two major projects, we are also collaborating with other Univ. of Washington faculty on molecular structures of importance for their functional studies. We currently have projects underway with Rachel Klevit (Biochemistry), Bill Parson (Biochemistry), Steve Libby (Laboratory Medicine), Steve Moseley (Microbiology), Evgeni Sokurenko (Microbiology), Bill Atkins (Medicinal Chemistry), and Rheem Totah (Medicinal Chemistry).

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