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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 1
Liu, Q1 1
Kriksunov, IA1 1
Campbell, AM2
Barrett, J2
Brophy, PM2
Hao, Q1 1
 
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