The Structure and Function of the PRMT5:MEP50 Complex.

Stephen Antonysamy

Journal: Sub-cellular biochemistry 2019;83():185-194

PMID: 28271477

Abstract

Protein arginine methyltransferase 5 (PRMT5) plays multiple roles in cellular processes at different stages of the cell cycle in a tissue specific manner. PRMT5 in complex with MEP50/p44/WDR77 associates with a plethora of partner proteins to symmetrically dimethylate arginine residues on target proteins in both the nucleus and the cytoplasm. Overexpression of PRMT5 has been observed in several cancers, making it an attractive drug target. The structure of the 453 kDa heterooctameric PRMT5:MEP50 complex bound to an S-adenosylmethionine analog and a substrate peptide provides valuable insights into this intriguing target.

Address: Structural Biology, Discovery Chemistry Research and Technologies, Eli Lilly and Company, Lilly Biotechnology Center, 10290 Campus Point Drive, San Diego, CA, 92121, USA. [email protected].

DOI: 10.1007/978-3-319-46503-6_7

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https://dx.doi.org/10.1007/978-3-319-46503-6_7

MeSH Terms: Adaptor Proteins, Signal Transducing, Arginine, Humans, Molecular Targeted Therapy, Multiprotein Complexes, Neoplasms, Protein-Arginine N-Methyltransferases, S-Adenosylmethionine, Substrate Specificity