File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus

TitleCrystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus
Authors
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
Citation
Proteins: Structure, Function And Genetics, 2005, v. 61 n. 4, p. 1024-1031 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/91915
ISSN
2015 Impact Factor: 2.499
2015 SCImago Journal Rankings: 1.383
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSchuller, DJen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorKriksunov, IAen_HK
dc.contributor.authorCampbell, AMen_HK
dc.contributor.authorBarrett, Jen_HK
dc.contributor.authorBrophy, PMen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:25Z-
dc.date.available2010-09-17T10:30:25Z-
dc.date.issued2005en_HK
dc.identifier.citationProteins: Structure, Function And Genetics, 2005, v. 61 n. 4, p. 1024-1031en_HK
dc.identifier.issn0887-3585en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91915-
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.en_HK
dc.languageengen_HK
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/36176en_HK
dc.relation.ispartofProteins: Structure, Function and Geneticsen_HK
dc.subjectCrystal structureen_HK
dc.subjectGlutathione transferase Nu2-2en_HK
dc.subjectLigand bindingen_HK
dc.subjectMolecular replacement methoden_HK
dc.titleCrystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrusen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/prot.20649en_HK
dc.identifier.pmid16189827en_HK
dc.identifier.scopuseid_2-s2.0-28644432297en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-28644432297&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume61en_HK
dc.identifier.issue4en_HK
dc.identifier.spage1024en_HK
dc.identifier.epage1031en_HK
dc.identifier.isiWOS:000233691100030-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSchuller, DJ=7102716051en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridKriksunov, IA=6507909504en_HK
dc.identifier.scopusauthoridCampbell, AM=7403505006en_HK
dc.identifier.scopusauthoridBarrett, J=7403498171en_HK
dc.identifier.scopusauthoridBrophy, PM=26643007200en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats