Snapshots of ispinesib-induced conformational changes in the mitotic kinesin eg5

Hung Yi Kristal Kaan, Jennifer Major, Katarzyna Tkocz, Frank Kozielski, Steven Rosenfeld

Research output: Contribution to journalArticle

15 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)18588-18598
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number25
DOIs
StatePublished - Jun 21 2013
Externally publishedYes

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Kinesin
Catalytic Domain
Neck
Switches
Molecules
ispinesib

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Snapshots of ispinesib-induced conformational changes in the mitotic kinesin eg5. / Kaan, Hung Yi Kristal; Major, Jennifer; Tkocz, Katarzyna; Kozielski, Frank; Rosenfeld, Steven.

In: Journal of Biological Chemistry, Vol. 288, No. 25, 21.06.2013, p. 18588-18598.

Research output: Contribution to journalArticle

Kaan, Hung Yi Kristal ; Major, Jennifer ; Tkocz, Katarzyna ; Kozielski, Frank ; Rosenfeld, Steven. / Snapshots of ispinesib-induced conformational changes in the mitotic kinesin eg5. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 25. pp. 18588-18598.
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