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- W4361866752 abstract "Laulimalide and peloruside A are microtubule-stabilizing agents (MSAs), the mechanism of action on microtubules of which is poorly defined. Here, using X-ray crystallography it is shown that laulimalide and peloruside A bind to a unique non-taxane site on β-tubulin and use their respective macrolide core structures to interact with a second tubulin dimer across protofilaments. At the same time, they allosterically stabilize the taxane-site M-loop that establishes lateral tubulin contacts in microtubules. Structures of ternary complexes of tubulin with laulimalide/peloruside A and epothilone A are also solved, and a crosstalk between the laulimalide/peloruside and taxane sites via the M-loop of β-tubulin is found. Together, the data define the mechanism of action of laulimalide and peloruside A on tubulin and microtubules. The data further provide a structural framework for understanding the synergy observed between two classes of MSAs in tubulin assembly and the inhibition of cancer cell growth." @default.
- W4361866752 created "2023-04-05" @default.
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- W4361866752 date "2014-01-27" @default.
- W4361866752 modified "2023-10-06" @default.
- W4361866752 title "Structural Basis of Microtubule Stabilization by Laulimalide and Peloruside A" @default.
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- W4361866752 doi "https://doi.org/10.1002/anie.201307749" @default.
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