A chemical probe for the methyl transferase PRMT5 with a novel binding mode was written by Pande, Vineet;Sun, Weimei;Beke, Lijs;Berthelot, Didier;Brehmer, Dirk;Brown, David;Corbera, Jordi;Irving, Steve;Meerpoel, Lieven;Nys, Thomas;Parade, Marc;Robinson, Colin;Sommen, Cois;Viellevoye, Marcel;Wu, Tongfei;Thuring, Jan Willem. And the article was included in ACS Medicinal Chemistry Letters in 2020.Related Products of 158078-04-7 The following contents are mentioned in the article:
Protein arginine methyltransferase 5 (PRMT5) is an enzyme that can sym. dimethylate arginine residues in histones and nonhistone proteins by using S-adenosyl methionine (SAM) as the Me donating cofactor. We have designed a library of SAM analogs and discovered potent, cell-active, and selective spiro diamines as inhibitors of the enzymic function of PRMT5. Crystallog. studies confirmed a very interesting binding mode, involving protein flexibility, where both the cofactor pocket and part of substrate binding site are occupied by these inhibitors. This study involved multiple reactions and reactants, such as ((3aR,4R,6R,6aR)-6-(4-Chloro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methanol (cas: 158078-04-7Related Products of 158078-04-7).
((3aR,4R,6R,6aR)-6-(4-Chloro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methanol (cas: 158078-04-7) belongs to dioxole derivatives. Dioxoles, particularly fluorinated dioxoles, are used as co-monomers to make polymers that find use in forming protective coatings for chemical resistance. Dioxole functionalized metal-organic frameworks have also been recently reported.Related Products of 158078-04-7
Referemce:
1,3-Benzodioxole – Wikipedia,
Dioxole | C3H4O2 – PubChem