March 27, 2019
Scott Lovell speaks on protein structures at today's Biochemistry and Molecular Biophysics Seminar
Scott Lovell, director of the Protein Structure Laboratory in the Del Shankel Structural Biology Center at the University of Kansas, will present "A Protein Structure Medley: From Functional Studies to Inhibitor Development" as part of the Biochemistry and Molecular Biophysics Seminar Series at 4 p.m. Wednesday, March 27, in 120 Ackert Hall.
Lovell earned his doctorate in organic chemistry and solid state chemistry from Purdue University in 2000. He followed this with two years as a postdoctoral research associate and staff scientist in protein crystallography at the University of Wisconsin. He has served six years managing a structural biology group in industry — deCODE biostructures, aka Emerald Biostructures — and was responsible for overseeing all aspects of gene-to-structure projects for external commercial clients and internal projects, focused on drug discovery and development. During this time, his laboratory maintained an overall success rate of 95 percent at obtaining inhibitor bound crystal structures for the projects under his supervision. In 2008, he became director of the Protein Structure Laboratory and, in 2012, a research professor in the department of molecular biosciences at the University of Kansas. He is a member of the American Crystallographic Association and the International Chemical Biology Society.
Lovell's protein structure laboratory collaborates consistently with investigators from various scientific disciplines. Therefore, the PSL often takes on projects that one could characterize as "routine" structure determination aimed at supporting a particular experiment over a short time period. Additionally, the PSL is often approached by investigators to collaborate on longer term projects that may span several months or years. As such, Lovell is currently a co-investigator on five NIH funded R01 grants for which he is responsible for managing the structural biology work to support inhibitor development.
X-ray crystallography is a commonly utilized technique for providing essential high-resolution structural information for researchers studying a variety of proteins. Details that can be obtained from a protein structure determination, that are often crucial to advancing a project, include metal binding characteristics, protein-protein interactions, protein-ligand interactions and inhibitor binding modes. Since X-ray crystallography is a somewhat specialized field, investigators routinely collaborate with structural biologists but are often unfamiliar with the techniques utilized to obtain structural information for proteins. As such, methods utilized for construct design, crystallization, X-ray data collection and computational aspects of crystallography will be addressed. Specific examples are presented that highlight the importance of obtaining structural information to gain mechanistic and functional insight for proteins. Additionally, the usefulness of incorporating structural biology techniques to probe the effects of small molecules on protein structure/function and to facilitate drug discovery efforts will be highlighted.