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      High-resolution crystal structure of Trypanosoma brucei UDP-galactose 4′-epimerase: a potential target for structure-based development of novel trypanocides

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      Molecular and Biochemical Parasitology
      Elsevier BV

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          Abstract

          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 A resolution (1 A = 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. Copyright 2002 Elsevier Science B.V.

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          Author and article information

          Journal
          Molecular and Biochemical Parasitology
          Molecular and Biochemical Parasitology
          Elsevier BV
          01666851
          February 2003
          February 2003
          : 126
          : 2
          : 173-180
          Article
          10.1016/S0166-6851(02)00243-8
          12615316
          ec16b458-3546-47b9-90b4-ac41b9bc64df
          © 2003

          https://www.elsevier.com/tdm/userlicense/1.0/

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