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Projects:

Neuropeptidase Function and Substrate Recognition Thimet oligopeptidase (TOP) is a zinc metallopeptidase that metabolizes a number of bioactive peptides and degrades peptides released by the proteasome, limiting antigenic presentation by MHC class I molecules. We present the crystal structure of human TOP at 2.0-Å resolution...

Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders Choline acetyltransferase (ChAT) synthesizes acetylcholine in neurons and other cell types. Decreases in ChAT activity are associated with a number of disease states, and mutations in ChAT cause congenital neuromuscular disorders...

Structure of neurolysin reveals a deep channel that limits substrate access The zinc metallopeptidase neurolysin is shown by x-ray crystallography to have large structural elements erected over the active site region that allow substrate access only through a deep narrow channel. This architecture accounts for...

Structures of nitroreductase in three states: Effects of inhibitor binding and reduction Nitroreductase is a member of a group of enzymes that reduce a broad range of nitroaromatic compounds and has potential uses in chemotherapy and bioremediation. In the oxidized enzyme, the flavin ring system adopts a strongly bent (16°) conformation...

     
 
Rodgers Research Group
Department of Molecular and Cellular Biochemistry
University of Kentucky
Biomedical Biological Sciences Research Building, Rm 236
741 South Limestone
Lexington, Ky 40356
859.323.8183 lab
859.323.1037 fax

 
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