Issue 1, 2011
From the journal:

Molecular BioSystems

A combinatorial approach to characterize the substrate specificity of proteinargininemethyltransferase 1†‡

Kevin L. Bicker,a   Obiamaka Obianyo,ab   Heather L. Rustab  and  Paul R. Thompson*ab  

* Corresponding authors

a Department of Chemistry and Biochemistry, University of South Carolina, 631 Sumter St., Columbia, South Carolina, USA

b Department of Chemistry, The Scripps Research Institute, Scripps Florida, 120 Scripps Way, Jupiter, Florida, USA
E-mail: Pthompso@scripps.edu
Fax: +1 561-228-3050
Tel: +1 561-228-2860

Abstract

The dysregulation of protein arginine methyltransferases (PRMTs) is implicated in a wide variety of disease states. Here we report the design, synthesis, and screening of a combinatorial peptide library used to characterize the substrate specificity of PRMT1. The information gained from this approach was used to develop a PRMT1 inhibitor with enhanced selectivity.

Graphical abstract: A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1

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Article information

DOI
https://doi.org/10.1039/C0MB00015A
Article type
Communication
Submitted
18 May 2010
Accepted
25 Jun 2010
First published
06 Jul 2010

Mol. BioSyst., 2011,7, 48-51

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A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1

K. L. Bicker, O. Obianyo, H. L. Rust and P. R. Thompson, Mol. BioSyst., 2011, 7, 48 DOI: 10.1039/C0MB00015A

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