API

Stressor: 124

Title

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Colchicine

Stressor Overview

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AOPs Including This Stressor

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Events Including This Stressor

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Event Name
Binding, Tubulin

Chemical Table

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AOP Evidence

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Chemical binding to tubulin in oocytes leading to aneuploid offspring

This is the prototype agent for binding to tubulin.

Colchicine binds at a site on tublulin known as the colchicine binding domain, which is a deep pocket located at the α/β interface of tubulin heterodimers. Both the A and C rings of colchicine are necessary for high affinity binding, while the B ring may only function as a linker between the other two. Three methoxy residues are present in the A ring and all of them are involved in the high affinity binding to tubulin. The C ring of colchicine interacts through van der Waals contacts with Valα181, Serα178, and Valβ315. The carbonyl group behaves as a hydrogen bond acceptor, interacting with Val181a. The A ring is buried in a hydrophobic pocket delimited by Lysβ352, Asnβ350, Leuβ378, Alaβ316, Leuβ255, Lysβ254, Alaβ250, and Leuβ242, and the methoxy group at position 3 is involved in a hydrogen bond interaction within the thiol group of Cysβ241 [Marchetti et al., 2016].




Event Evidence

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Binding, Tubulin

There is no evidence text for this event.




Stressor Info

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Chemical/Category Description

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Characterization of Exposure

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References

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