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Structural Basis of Splicing Modulation by Antitumor Macrolide Compounds.

Constantin Cretu1, Anant A Agrawal2, Andrew Cook2

  • 1Research Group Macromolecular Crystallography, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

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Summary

Pladienolide B (PB) binds the SF3B complex, a key splicing factor, and halts its function. This structural insight into PB

Keywords:
A complexSF3balternative splicingantitumor drugbranch sitepre-mRNA splicingspliceosomesplicing modulator

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Drug Discovery

Background:

  • The SF3B complex is crucial for pre-mRNA splicing, specifically branch site recognition.
  • Splicing modulators, including those with antitumor activity, interact with SF3B.
  • Understanding SF3B-modulator interactions is key for developing new cancer therapies.

Purpose of the Study:

  • To determine the crystal structure of the human SF3B core in complex with pladienolide B (PB).
  • To elucidate the molecular mechanism by which PB modulates SF3B function.
  • To provide a structural basis for designing novel SF3B-targeting drugs.

Main Methods:

  • X-ray crystallography was used to obtain the high-resolution structure of the SF3B core-PB complex.
  • Biochemical assays were employed to assess the impact of PB on SF3B conformation and splicing activity.
  • Structural analysis focused on identifying key interactions between PB and SF3B.

Main Results:

  • The crystal structure reveals PB wedges into the SF3B hinge, stalling the complex in an open conformation.
  • This open conformation prevents SF3B from transitioning to the closed state required for branch site binding.
  • Key interactions between PB and SF3B define a common pharmacophore relevant to splicing modulation.

Conclusions:

  • Pladienolide B inhibits SF3B by stabilizing an open conformation, thereby disrupting pre-mRNA splicing.
  • The determined structure provides a detailed molecular understanding of PB's mechanism of action.
  • This research offers a structural framework for the rational design of next-generation splicing modulators for cancer treatment.