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Related Experiment Video

Updated: Feb 13, 2026

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Cryo-electron microscopy structure of a human PRMT5:MEP50 complex.

David E Timm1, Valorie Bowman2, Russell Madsen3

  • 1Structural Biology, Discovery Chemistry Research and Technologies, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, Indiana, United States of America.

Plos One
|March 9, 2018
PubMed
Summary

A cryo-EM structure of Protein Arginine Methyltransferase 5 (PRMT5) complexed with MEP50 was determined. This structure reveals key details of the hetero-octameric assembly and a bound inhibitor, showcasing cryo-EM

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Protein Arginine Methyltransferase 5 (PRMT5) is a key signaling protein and histone modifying enzyme.
  • PRMT5 plays a crucial role in regulating eukaryotic gene transcription and other cellular processes.

Purpose of the Study:

  • To determine the high-resolution structure of the PRMT5-MEP50 complex using cryo-EM.
  • To visualize the hetero-octameric assembly and interactions within the complex.
  • To identify bound inhibitor molecules for potential therapeutic insights.

Main Methods:

  • Single particle cryo-electron microscopy (cryo-EM) was employed to solve the structure.
  • Micrographs of aggregated particles were processed to obtain a 3.7 Å resolution reconstruction.
  • The structure was analyzed for subunit arrangement, symmetry, and inhibitor binding.

Main Results:

  • A 3.7 Å cryo-EM structure of the 450 kDa PRMT5-MEP50 hetero-octameric complex was obtained.
  • The structure revealed a core tetramer of PRMT5 subunits with peripheral MEP50 subunits.
  • A dehydrosinefungin inhibitor molecule was well-resolved, bound to the complex.

Conclusions:

  • Cryo-EM is effective for determining the structure of large human protein complexes, even with suboptimal sample conditions.
  • The determined structure provides insights into PRMT5 complex organization and inhibitor interaction.
  • Cryo-EM can be further applied to study PRMT5 interactions with other binding partners and ligands.