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Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus.

Proteins

Strongylida Infections, Animals, Protein Structure, Secondary, Models, Molecular, Ligands, Humans, enzymology, Heligmosomatoidea, metabolism, chemistry, antagonists & inhibitors, Glutathione Transferase, pharmacology, Enzyme Inhibitors, Crystallography, X-Ray, Binding Sites

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      Abstract

      The crystal structure of GST Nu2-2 (HpolGSTN2-2) from the model hookworm nematode Heligmosomoides polygyrus has been solved by the molecular replacement method and refined to a resolution of 1.71 A, providing the first structural data from a class of nematode-specific GSTs. By structural alignment with two Sigma class GSTs, glutathione could be rationally docked into the G-site of the enzyme. By comparing with all mammalian GST classes, a novel, long, and deep cleft was identified at the H-site, providing a potential site for ligand binding. This new GST class may support the establishment of infection parasitic nematodes by passively neutralizing chemical toxins derived from host environment. The structure serves as a starting point for structure-based drug/inhibitor design that would aim to selectively disrupt nematode chemical defenses. Proteins 2005. 2005 Wiley-Liss, Inc.

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      Journal
      10.1002/prot.20649
      16189827

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