We propose to collect native and derivative data from crystals of two enzymes that form part of the purine salvage pathway of the parasitic protozoan Tritrichomomas foetus. One of these enzymes, Inosine Monophosphate Dehydrogenase (IMPDH) catalyzes the NAD-dependent oxidation of inosine monophosphate (IMP) to xanthine monophosphate (XMP). The structure of this enzyme will be the first IMPDH structure determined and it will serve as a model in determining the structures of both of the human IMPDH isoforms. Under a variety of circumstances, IMPDH represents an attractive target for the design of specific inhibitors which are likely to be very effective in the treatment of cancer, in preventing tissue rejection, as an antiviral agent, and in the control of parasitic infections of humans and livestock.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-22
Application #
6437511
Study Section
Project Start
2001-03-01
Project End
2002-02-28
Budget Start
Budget End
Support Year
22
Fiscal Year
2001
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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