Home
Resources
Publications
Functional Insights From High Resolution Structures of Mouse Protein Arginine Methyltransferase 6

Functional Insights From High Resolution Structures of Mouse Protein Arginine Methyltransferase 6

Luc Bonnefond, Johann Stojko, Justine Mailliot, Nathalie Troffer-Charlier, Vincent Cura, Jean-Marie Wurtz, Sarah Cianférani, Jean Cavarelli

J Struct Biol. 2015 Aug;191(2):175-83.

PMID: 26094878

Abstract:

PRMT6 is a protein arginine methyltransferase involved in transcriptional regulation, human immunodeficiency virus pathogenesis, DNA base excision repair, and cell cycle progression. Like other PRMTs, PRMT6 is overexpressed in several cancer types and is therefore considered as a potential anti-cancer drug target. In the present study, we described six crystal structures of PRMT6 from Mus musculus, solved and refined at 1.34 Å for the highest resolution structure. The crystal structures revealed that the folding of the helix αX is required to stabilize a productive active site before methylation of the bound peptide can occur. In the absence of cofactor, metal cations can be found in the catalytic pocket at the expected position of the guanidinium moiety of the target arginine substrate. Using mass spectrometry under native conditions, we show that PRMT6 dimer binds two cofactor and a single H4 peptide molecules. Finally, we characterized a new site of in vitro automethylation of mouse PRMT6 at position 7.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416114	PRMT6 active human			Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: