(S)-monastrol and monastrol

(S)-monastrol has been researched along with monastrol* in 2 studies

*monastrol: stops mitosis by fostering formation of monopolar spindles; structure in first source [MeSH]

Other Studies

2 other study(ies) available for (S)-monastrol and monastrol

Article	Year
Monastrol, a 3,4-dihydropyrimidin-2(1H)-thione, as structural scaffold for the development of modulators for GHB high-affinity binding sites and α European journal of medicinal chemistry, 2017, Sep-29, Volume: 138 The α Topics: Binding Sites; Dose-Response Relationship, Drug; Humans; Molecular Structure; Pyrimidines; Receptors, GABA-A; Structure-Activity Relationship; Thiones	2017
Inhibition of a mitotic motor protein: where, how, and conformational consequences. Journal of molecular biology, 2004, Jan-09, Volume: 335, Issue:2 We report here the first inhibitor-bound structure of a mitotic motor protein. The 1.9 A resolution structure of the motor domain of KSP, bound with the small molecule monastrol and Mg2+ x ADP, reveals that monastrol confers inhibition by "induced-fitting" onto the protein some 12 A away from the catalytic center of the enzyme, resulting in the creation of a previously non-existing binding pocket. The structure provides new insights into the biochemical and mechanical mechanisms of the mitotic motor domain. Inhibition of KSP provides a novel mechanism to arrest mitotic spindle formation, a target of several approved and investigative anti-cancer agents. The structural information gleaned from this novel pocket offers a new angle for the design of anti-mitotic agents. Topics: Adenosine Diphosphate; Binding Sites; Crystallization; Crystallography, X-Ray; Humans; Kinesins; Magnesium; Microtubules; Mitosis; Models, Molecular; Molecular Motor Proteins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Pyrimidines; Structure-Activity Relationship; Thiones	2004

Article

Year

Monastrol, a 3,4-dihydropyrimidin-2(1H)-thione, as structural scaffold for the development of modulators for GHB high-affinity binding sites and α

European journal of medicinal chemistry, 2017, Sep-29, Volume: 138

The α

Topics: Binding Sites; Dose-Response Relationship, Drug; Humans; Molecular Structure; Pyrimidines; Receptors, GABA-A; Structure-Activity Relationship; Thiones

2017

Inhibition of a mitotic motor protein: where, how, and conformational consequences.

Journal of molecular biology, 2004, Jan-09, Volume: 335, Issue:2

We report here the first inhibitor-bound structure of a mitotic motor protein. The 1.9 A resolution structure of the motor domain of KSP, bound with the small molecule monastrol and Mg2+ x ADP, reveals that monastrol confers inhibition by "induced-fitting" onto the protein some 12 A away from the catalytic center of the enzyme, resulting in the creation of a previously non-existing binding pocket. The structure provides new insights into the biochemical and mechanical mechanisms of the mitotic motor domain. Inhibition of KSP provides a novel mechanism to arrest mitotic spindle formation, a target of several approved and investigative anti-cancer agents. The structural information gleaned from this novel pocket offers a new angle for the design of anti-mitotic agents.

Topics: Adenosine Diphosphate; Binding Sites; Crystallization; Crystallography, X-Ray; Humans; Kinesins; Magnesium; Microtubules; Mitosis; Models, Molecular; Molecular Motor Proteins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Pyrimidines; Structure-Activity Relationship; Thiones

2004