Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s) | Zendy

Julia R. Ellis | Zendy; Richard E. Taylor | Zendy; Patrick J. Hussey | Zendy

Open Access

Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s)

Author(s) -

Julia R. Ellis,

Richard E. Taylor,

Patrick J. Hussey

Publication year - 1994

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.105.1.15

Subject(s) - microtubule , mitosis , tubulin , biology , plant cell , biophysics , spindle apparatus , microbiology and biotechnology , binding site , chemistry , cell , biochemistry , cell division , gene

Dinitroaniline and phosphorothioamidate herbicides disrupt microtubule assembly from tubulin protein dimers and thereby halt microtubule-based processes such as mitosis in plant cells. Despite the contrasting chemical properties of dinitroaniline and phosphorothioamidate herbicides, a three-dimensional molecular analysis revealed remarkable electrostatic similarity between these two classes of herbicide. From these data it is proposed that dinitroaniline and phosphorothioamidate herbicides share common binding site(s) in the plant cell.

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