1tw9

Publication Abstract from PubMed

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.

Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus.,Schuller DJ, Liu Q, Kriksunov IA, Campbell AM, Barrett J, Brophy PM, Hao Q Proteins. 2005 Dec 1;61(4):1024-31. PMID:16189827^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.