期刊
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
卷 126, 期 2, 页码 173-180出版社
ELSEVIER
DOI: 10.1016/S0166-6851(02)00243-8
关键词
epimerase; galactose; Trypanosoma brucei; UDP-Gal; X-ray structure
The crystal structure of UDP-galactose 4'-epimerase from the protozoan parasite Trypanosoma brucei in complex with the cofactor NAD(+) and a fragment of the substrates, UDP, has been determined at 2.0 Angstrom resolution (1 Angstrom = 0.1 nm). This enzyme, recently proven to be essential for this pathogenic parasite, shares 33% sequence identity with the corresponding enzyme in the human host. Structural comparisons indicate that many of the protein-ligand interactions are conserved between the two enzymes. However, in the UDP-binding pocket there is a non-conservative substitution from Gly237 in the human enzyme to Cys266 in the T. brucei enzyme. Such a significant difference could be exploited by the structure-based design of selective inhibitors using the structure of the trypanosomatid enzyme as a template. (C) 2002 Elsevier Science B.V. All rights reserved.
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