AOPs Including This Stressor
|Chemical binding to tubulin in oocytes leading to aneuploid offspring||High|
Events Including This Stressor
|User term||DTXID||Preferred name||Casrn||jchem_inchi_key||indigo_inchi_key|
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].
There is no evidence text for this event.