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245 1 0 _aA possible model of benzimidazole binding to b-tubulin disclosed by invoking an inter-domain movement
490 0 _vJournal of Molecular Graphics and Modelling, 23(3), p.275-284, 2004
520 3 _aAlthough it is well established that benzimidazole (BZMs)compounds exert their therapeutic effects through binding to helminth btubulin and thus disrupting microtubule-based processes in the parasites, the precise location of the benzimidazole-binding site on the btubulin molecule has yet to be determined. In the present study, we have used previous experimental data as cues to help identify this site. Firstly, benzimidazole resistance has been correlated with a phenylalanine-to-tyrosine substitution at position 200 of Haemonchus contortus b-tubulin isotype-I. Secondly, site-directed mutagenesis studies, using fungi, have shown that other residues in this region of the protein can influence the interaction of benzimidazoles with b-tubulin. However, the atomic structure of the ab-tubulin dimer shows that residue 200 and the other implicated residues are buried within the protein. This poses the question: how might benzimidazoles interact with these apparently inaccessible residues? In the present study, we present a mechanism by which those residues generally believed to interact with benzimidazoles may become accessible to the drugs. Furthermore, by docking albendazole-sulphoxide into a modelled H. contortus btubulin molecule we offer a structural explanation for how the mutation conferring benzimidazole resistance in nematodes may act, as well as a possible explanation for the species-specificity of benzimidazole anthelmintics.
650 1 4 _aBENZIMIDAZOLE
650 1 4 _aTUBULIN
650 1 4 _aBENZIMIDAZOLE RESISTANCE
650 1 4 _aDOMAIN MOVEMENT
650 1 4 _aHAEMONCHUS CONTORTUS
650 1 4 _aFASCIOLA HEPATICA
700 1 2 _aRobinson, M.W.
700 1 2 _aMcferran, N.
700 1 2 _aTrudgett, A.
700 1 2 _aHoey, L.
700 1 2 _aFairweather, I.
856 4 0 _uhttps://drive.google.com/file/d/1budK0m1C3Z4wkbC-DM4NmCxjhaXFBcn2/view?usp=drivesdk
_zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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