CRYSTAL STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM EUKARYOTIC PATHOGENS
Cornell University, Ithaca NY
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Abstract
This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Infectious diseases are a major world health problem and developing new antibiotics remains a critical field of research. Eukaryotic pathogens are less well understood than bacterial ones, but infect hundreds of millions of people world-wide. These diseases include leishmaniasis, Chaga's disease, African sleeping sickness and invasive aspergillosis. Eukaryotic pathogens are difficult to develop antibiotics against because they are fairly similar to humans. A potential target is UDP-galactopyranose mutase (UGM), which catalyzes the interconversion of UDP galactopyranose (UDP Galp;6 membered ring) and UDP-galactofuranose (UDP Galf;5 membered ring). UDP Galf is the precursor for galactofuranose (Galf) sugar residues found in cell wall components. We are currently studying the structure-function of this enzyme from the pathogenic eukaryotes Leishmania and Aspergillus.
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