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dc.contributor.author Schuller, David J.
dc.contributor.author Liu, Qun
dc.contributor.author Kriksunov, Irina A.
dc.contributor.author Campbell, Alison M.
dc.contributor.author Barrett, John
dc.contributor.author Brophy, Peter M.
dc.contributor.author Hao, Quan
dc.date.accessioned 2009-11-30T11:32:46Z
dc.date.available 2009-11-30T11:32:46Z
dc.date.issued 2005-12-01
dc.identifier.citation Schuller , D J , Liu , Q , Kriksunov , I A , Campbell , A M , Barrett , J , Brophy , P M & Hao , Q 2005 , ' Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus ' Proteins: Structure, Function, and Bioinformatics , vol 61 , no. 4 , pp. 1024-1031 . , 10.1002/prot.20649 en
dc.identifier.issn 0887-3585
dc.identifier.other PURE: 140899
dc.identifier.other dspace: 2160/3727
dc.identifier.uri http://hdl.handle.net/2160/3727
dc.description Schuller, D. J., Liu, Q., Kriksunov, I. A., Campbell, A. M., Barrett, J., Brophy, P. M., Hao, Q. (2005). Crystal structure of a new class of glutathione transferase from the model human hookworm ematode Heligmosomoides polygyrus. Proteins: Structure Function and Bioinformatics, 61, (4), 1024-1031. Sponsorship: BBSRC UK-Grant Number: S14953/ National Institutes of Health (National Center for Research Resources)-Grant Number: RR-01646/ National Science Foundation - Grant Number: DMR 02-25180. en
dc.description.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. en
dc.format.extent 8 en
dc.language.iso eng
dc.relation.ispartof Proteins: Structure, Function, and Bioinformatics en
dc.subject Keywords: glutathione transferase Nu2-2 en
dc.subject molecular replacement method en
dc.subject ligand binding en
dc.subject crystal structure en
dc.title Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1002/prot.20649
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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