Article
Mutations in the human kinesin Eg5 that confer resistance to monastrol and S-trityl-L-cysteine in tumor derived cell lines.
Biochemical pharmacology - 15 Mar 2010
Tcherniuk Sergey, van Lis Robert, Kozielski Frank, Skoufias Dimitrios A
Abstract excerpt
The kinesin Eg5 plays an essential role in bipolar spindle formation. A variety of structurally diverse inhibitors of the human kinesin Eg5, including monastrol and STLC, share the same binding pocket on Eg5, composed by helix alpha2/loop L5, and helix alpha3 of the Eg5 motor domain. Previous biochemical analysis in the inhibitor binding pocket of Eg5 identified key residues in the inhibitor binding pocket of Eg5...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
