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Related Experiment Video

Updated: May 17, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Published on: May 13, 2020

Crystal structure of the human PRMT5:MEP50 complex.

Stephen Antonysamy¹, Zahid Bonday, Robert M Campbell

¹Lilly Biotechnology Center, Eli Lilly and Company, San Diego, CA 92121, USA.

Proceedings of the National Academy of Sciences of the United States of America

|October 17, 2012

Summary

This study reveals the crystal structure of human PRMT5 complexed with MEP50, detailing their interaction and substrate recognition. This provides insights into protein arginine methyltransferase 5 (PRMT5) function in cellular processes.

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Area of Science:

Biochemistry and structural biology
Molecular and cellular biology

Background:

Protein arginine methyltransferases (PRMTs) are crucial enzymes regulating cellular processes like gene expression and signaling.
PRMT5 specifically performs symmetric di-methylation of arginine residues, impacting cell growth and development.
MEP50 (methylosome protein 50) is a key WD40 protein that forms a core component of PRMT5 complexes, mediating interactions.

Purpose of the Study:

To determine the crystal structure of the human PRMT5-MEP50 complex.
To elucidate the structural basis of substrate recognition and the interaction between PRMT5 and MEP50.

Main Methods:

X-ray crystallography was employed to determine the structure of the human PRMT5-MEP50 complex.
The complex was studied in the presence of an S-adenosylmethionine analog and a peptide substrate derived from histone H4.

Main Results:

The crystal structure of a hetero-octameric complex comprising human PRMT5 and MEP50 was determined.
The structure highlights close interactions between the WD40 protein MEP50 and the N-terminal domain of PRMT5.
Key structural elements involved in substrate recognition by the PRMT5-MEP50 complex were identified.

Conclusions:

The determined structure provides a detailed molecular understanding of the PRMT5-MEP50 complex.
This structural information is vital for comprehending PRMT5's role in cellular functions and for potential therapeutic targeting.