Benzimidazole binding to Haemonchus contortus tubulin: a question of structure.

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Show simple item record Robinson, MW Trudgett, A Fairweather, I McFerran, N 2011-02-07T06:29:09Z 2002-01
dc.identifier.citation Trends in Parasitology, 2002, 18 (4), pp. 153 - 154
dc.identifier.issn 1471-4922
dc.identifier.other C4 en_US
dc.description.abstract The September 2001 issue of Trends in Parasitology had a review entitled `Genetic variability following selection of Haemonchus contortus with anthelmintics, by Roger K. Prichard [1]. This included a diagrammatic representation of the proposed benzimidazole (BZM) binding to H. contortus tubulin, presumably based on the electron diffraction structure of porcine tubulin ?-chain [2], although this was not stated. It was suggested that BZM dock with the tubulin molecule within a site formed by four residues on the tubulin ?-chain (Ser166, Phe167, Phe200 and Cys201). We concur that these four ?-tubulin residues cluster together in the published model of the three-dimensional conformation of the protein; however, using this structure, we find the proposed BZM docking to be questionable on the following grounds.
dc.format Yes
dc.publisher Elsevier Inc
dc.relation.isbasedon 10.1016/S1471-4922(01)02225-5
dc.title Benzimidazole binding to Haemonchus contortus tubulin: a question of structure.
dc.type Journal Article
dc.parent Trends in Parasitology
dc.journal.volume 4
dc.journal.volume 18
dc.journal.number 4 en_US
dc.publocation Oxford, UK en_US
dc.identifier.startpage 153 en_US
dc.identifier.endpage 154 en_US SCI.Institute for Biotechnology of Infectious Diseases en_US
dc.conference Verified OK en_US
dc.for 0605 Microbiology
dc.personcode 100777
dc.percentage 100 en_US Microbiology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US en_US
dc.location.activity en_US
dc.description.keywords en_US
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
utslib.copyright.status Closed Access 2015-04-15 12:17:09.805752+10
utslib.collection.history Closed (ID: 3)
utslib.collection.history Uncategorised (ID: 363)

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