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Related Experiment Videos

Inhibitors of kinesin activity from structure-based computer screening.

S C Hopkins1, R D Vale, I D Kuntz

  • 1Department of Pharmaceutical Chemistry, Howard Hughes Medical Institute, University of California, San Francisco, California 94143-0446, USA. seth@itsa.ucsf.edu

Biochemistry
|March 8, 2000
PubMed
Summary
This summary is machine-generated.

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Researchers identified novel small organic molecules that inhibit kinesin motor protein activity. These compounds target a specific pocket involved in microtubule binding, offering new avenues for therapeutic development.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Kinesin motor proteins are essential for intracellular transport, utilizing ATP hydrolysis.
  • Inhibiting kinesin activity is a potential therapeutic strategy.

Purpose of the Study:

  • To identify small organic ligands that inhibit kinesin's ATPase activity.
  • To characterize the binding site and mechanism of inhibition.

Main Methods:

  • Computational docking (DOCK program) of commercially available compounds.
  • Assay of microtubule-stimulated ATPase activity.
  • Fluorescence anisotropy and FRET for binding site localization.

Main Results:

  • Identified 22 submillimolar kinesin inhibitors, falling into four chemical classes.

Related Experiment Videos

  • Three compounds exhibited single-digit micromolar inhibition.
  • Rose bengal lactone (RBL) binds to a novel pocket involving loop 8 and beta-strand 5, crucial for microtubule interaction.

    • Conclusions:

    • A novel binding pocket in kinesin, distinct from the ATP site, has been identified for inhibitor development.
    • These findings provide a basis for designing targeted kinesin inhibitors.