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Article: Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus
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TitleCrystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus
 
AuthorsSchuller, DJ1
Liu, Q1
Kriksunov, IA1
Campbell, AM2
Barrett, J2
Brophy, PM2
Hao, Q1
 
KeywordsCrystal structure
Glutathione transferase Nu2-2
Ligand binding
Molecular replacement method
 
Issue Date2005
 
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/36176
 
CitationProteins: Structure, Function And Genetics, 2005, v. 61 n. 4, p. 1024-1031 [How to Cite?]
DOI: http://dx.doi.org/10.1002/prot.20649
 
AbstractThe 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. © 2005 Wiley-Liss, Inc.
 
ISSN0887-3585
2012 Impact Factor: 3.337
2012 SCImago Journal Rankings: 1.754
 
DOIhttp://dx.doi.org/10.1002/prot.20649
 
ISI Accession Number IDWOS:000233691100030
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSchuller, DJ
 
dc.contributor.authorLiu, Q
 
dc.contributor.authorKriksunov, IA
 
dc.contributor.authorCampbell, AM
 
dc.contributor.authorBarrett, J
 
dc.contributor.authorBrophy, PM
 
dc.contributor.authorHao, Q
 
dc.date.accessioned2010-09-17T10:30:25Z
 
dc.date.available2010-09-17T10:30:25Z
 
dc.date.issued2005
 
dc.description.abstractThe 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. © 2005 Wiley-Liss, Inc.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationProteins: Structure, Function And Genetics, 2005, v. 61 n. 4, p. 1024-1031 [How to Cite?]
DOI: http://dx.doi.org/10.1002/prot.20649
 
dc.identifier.doihttp://dx.doi.org/10.1002/prot.20649
 
dc.identifier.epage1031
 
dc.identifier.isiWOS:000233691100030
 
dc.identifier.issn0887-3585
2012 Impact Factor: 3.337
2012 SCImago Journal Rankings: 1.754
 
dc.identifier.issue4
 
dc.identifier.pmid16189827
 
dc.identifier.scopuseid_2-s2.0-28644432297
 
dc.identifier.spage1024
 
dc.identifier.urihttp://hdl.handle.net/10722/91915
 
dc.identifier.volume61
 
dc.languageeng
 
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/36176
 
dc.publisher.placeUnited States
 
dc.relation.ispartofProteins: Structure, Function and Genetics
 
dc.relation.referencesReferences in Scopus
 
dc.subjectCrystal structure
 
dc.subjectGlutathione transferase Nu2-2
 
dc.subjectLigand binding
 
dc.subjectMolecular replacement method
 
dc.titleCrystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus
 
dc.typeArticle
 
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Author Affiliations
  1. Cornell University
  2. University of Wales Aberystwyth