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 Å, 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.
Original language | English |
---|---|
Pages (from-to) | 1024-1031 |
Number of pages | 8 |
Journal | Proteins: Structure, Function and Genetics |
Volume | 61 |
Issue number | 4 |
Early online date | 27 Sept 2005 |
DOIs | |
Publication status | Published - 01 Dec 2005 |
Keywords
- Keywords: glutathione transferase Nu2-2
- molecular replacement method
- ligand binding
- crystal structure