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- Publisher Website: 10.1002/prot.20649
- Scopus: eid_2-s2.0-28644432297
- PMID: 16189827
- WOS: WOS:000233691100030
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Article: Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus
Title | Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus |
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Authors | |
Keywords | Crystal structure Glutathione transferase Nu2-2 Ligand binding Molecular replacement method |
Issue Date | 2005 |
Publisher | John 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? |
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. © 2005 Wiley-Liss, Inc. |
Persistent Identifier | http://hdl.handle.net/10722/91915 |
ISSN | 2021 Impact Factor: 4.088 2020 SCImago Journal Rankings: 1.699 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Schuller, DJ | en_HK |
dc.contributor.author | Liu, Q | en_HK |
dc.contributor.author | Kriksunov, IA | en_HK |
dc.contributor.author | Campbell, AM | en_HK |
dc.contributor.author | Barrett, J | en_HK |
dc.contributor.author | Brophy, PM | en_HK |
dc.contributor.author | Hao, Q | en_HK |
dc.date.accessioned | 2010-09-17T10:30:25Z | - |
dc.date.available | 2010-09-17T10:30:25Z | - |
dc.date.issued | 2005 | en_HK |
dc.identifier.citation | Proteins: Structure, Function And Genetics, 2005, v. 61 n. 4, p. 1024-1031 | en_HK |
dc.identifier.issn | 0887-3585 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/91915 | - |
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. © 2005 Wiley-Liss, Inc. | en_HK |
dc.language | eng | en_HK |
dc.publisher | John Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/36176 | en_HK |
dc.relation.ispartof | Proteins: Structure, Function and Genetics | en_HK |
dc.subject | Crystal structure | en_HK |
dc.subject | Glutathione transferase Nu2-2 | en_HK |
dc.subject | Ligand binding | en_HK |
dc.subject | Molecular replacement method | en_HK |
dc.title | Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Hao, Q: qhao@hku.hk | en_HK |
dc.identifier.authority | Hao, Q=rp01332 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1002/prot.20649 | en_HK |
dc.identifier.pmid | 16189827 | en_HK |
dc.identifier.scopus | eid_2-s2.0-28644432297 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-28644432297&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 61 | en_HK |
dc.identifier.issue | 4 | en_HK |
dc.identifier.spage | 1024 | en_HK |
dc.identifier.epage | 1031 | en_HK |
dc.identifier.isi | WOS:000233691100030 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Schuller, DJ=7102716051 | en_HK |
dc.identifier.scopusauthorid | Liu, Q=35215401600 | en_HK |
dc.identifier.scopusauthorid | Kriksunov, IA=6507909504 | en_HK |
dc.identifier.scopusauthorid | Campbell, AM=7403505006 | en_HK |
dc.identifier.scopusauthorid | Barrett, J=7403498171 | en_HK |
dc.identifier.scopusauthorid | Brophy, PM=26643007200 | en_HK |
dc.identifier.scopusauthorid | Hao, Q=7102508868 | en_HK |
dc.identifier.issnl | 0887-3585 | - |