Abstract
Background: Ispinesib is a small molecule inhibitor of Eg5 and induces neck linker docking. Results: Ispinesib binding to Eg5 induces subsequent movement of switch II. Conclusion: Conformational changes in L5 can alter the orientation of the neck linker regardless of the state of the catalytic site. Significance: L5 is a key regulator of both the catalytic site and switch II.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 18588-18598 |
| Number of pages | 11 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 25 |
| DOIs | |
| State | Published - Jun 21 2013 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Kaan, H. Y. K., Major, J., Tkocz, K., Kozielski, F., & Rosenfeld, S. S. (2013). Snapshots of ispinesib-induced conformational changes in the mitotic kinesin eg5. Journal of Biological Chemistry, 288(25), 18588-18598. https://doi.org/10.1074/jbc.M113.462648