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

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Show simple item record Robinson, Mark en_US Trudgett, A en_US Fairweather, I en_US Mcferran, Neil en_US
dc.contributor.editor en_US 2011-02-07T06:29:09Z 2011-02-07T06:29:09Z 2002 en_US
dc.identifier 2009005087 en_US
dc.identifier.citation Robinson Mark et al. 2002, 'Benzimidazole binding to Haemonchus contortus tubulin: a question of structure.', Trends in Parasitology, Elsevier Inc, Oxford, UK en_US
dc.identifier.issn 1471-4922 en_US
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. en_US
dc.language en_US
dc.publisher Elsevier Inc en_US
dc.relation.isbasedon en_US
dc.title Benzimidazole binding to Haemonchus contortus tubulin: a question of structure. en_US
dc.parent Trends in Parasitology en_US
dc.journal.volume 18 en_US
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 060500 en_US
dc.personcode 100777 en_US
dc.personcode 0000033423 en_US
dc.personcode 0000033422 en_US
dc.personcode 0000062058 en_US
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

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