10.1021/jm061213n.s001
Rino Ragno
Rino
Ragno
Silvia Simeoni
Silvia
Simeoni
Sabrina Castellano
Sabrina
Castellano
Caterina Vicidomini
Caterina
Vicidomini
Antonello Mai
Antonello
Mai
Antonella Caroli
Antonella
Caroli
Anna Tramontano
Anna
Tramontano
Claudia Bonaccini
Claudia
Bonaccini
Patrick Trojer
Patrick
Trojer
Ingo Bauer
Ingo
Bauer
Gerald Brosch
Gerald
Brosch
Gianluca Sbardella
Gianluca
Sbardella
Small Molecule Inhibitors of Histone Arginine Methyltransferases: Homology Modeling,
Molecular Docking, Binding Mode Analysis, and Biological Evaluations
American Chemical Society
2007
binding mode analyses
Aspergillus nidulans RmtA
modeling
Biological EvaluationsThe screening
QSAR
Small Molecule Inhibitors
screening arginine methyltransferase inhibitors
novel PRMT inhibitors
PRMT 1
Binding Mode Analysis
region
SAM cisteinic binding site subsite
2007-03-22 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Small_Molecule_Inhibitors_of_Histone_Arginine_Methyltransferases_Homology_Modeling_Molecular_Docking_Binding_Mode_Analysis_and_Biological_Evaluations/3017209
The screening of the inhibition capabilities of dye-like small molecules from a focused library against both
human PRMT1 and <i>Aspergillus </i><i>nidulans</i> RmtA is reported as well as molecular modeling studies (homology
modeling, molecular docking, and 3-D QSAR) of the catalytic domain of the PRMT1 fungal homologue
RmtA. The good correlation between computational and biological results makes RmtA a reliable tool for
screening arginine methyltransferase inhibitors. In addition, the binding mode analyses of tested derivatives
reveal the crucial role of two regions, the pocket formed by Ile12, His13, Met16, and Thr49 and the SAM
cisteinic binding site subsite. These regions should be taken into account in the design of novel PRMT
inhibitors.