Literature summary for 2.1.1.319 extracted from

Bonnefond, L.; Stojko, J.; Mailliot, J.; Troffer-Charlier, N.; Cura, V.; Wurtz, J.M.; Cianferani, S.; Cavarelli, J.
Functional insights from high resolution structures of mouse protein arginine methyltransferase 6 (2015), J. Struct. Biol., 191, 175-183 .

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Cloned(Commentary)

Cloned (Comment)	Organism
prmt6 is cloned in the pnEA-vHis vector between the NdeI and XhoI restriction sites and used to transform Escherichia coli BL21 (DE3) pRARE2 cells. The resulting recombinant protein harbors an amino-terminal hexahistidine tag followed by a Tobacco etch virus (TEV) protease cleavage site. The protein also contains a F315L point mutation, reported for the entry as a natural variant	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapor-diffusion method at 20°C. Six crystal structures of PRMT6 are solved and refined at 1.34 A for the highest resolution structure.The crystal structures reveal that the folding of the helix aX 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	Mus musculus

Crystallization (Comment)

Organism

sitting-drop vapor-diffusion method at 20°C. Six crystal structures of PRMT6 are solved and refined at 1.34 A for the highest resolution structure.The crystal structures reveal that the folding of the helix aX 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

Mus musculus

Protein Variants

Protein Variants	Comment	Organism
F315L	point mutation of a natural variant	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q6NZB1	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Mus musculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 S-adenosyl-L-methionine + [histone H4R3]-L-arginine	-	Mus musculus	2 S-adenosyl-L-homocysteine + [histone H4R3]-Nomega,Nomega-dimethyl-L-arginine	-	?
2 S-adenosyl-L-methionine + [protein]-L-arginine	a site of in vitro automethylation of mouse PRMT6 is characterized at position 7	Mus musculus	2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega-dimethyl-L-arginine	-	?

Synonyms

Synonyms	Comment	Organism
PRMT6	-	Mus musculus
protein arginine methyltransferase 6	-	Mus musculus

General Information

General Information	Comment	Organism
drug target	PRMT6 is overexpressed in several cancer types and is therefore considered as a potential anti-cancer drug target	Mus musculus
physiological function	the enzyme (PRMT6) is a protein arginine methyltransferase involved in transcriptional regulation, human immunodeficiency virus pathogenesis, DNA base excision repair, and cell cycle progression	Mus musculus