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• W2117892897 endingPage "3519" @default.
• W2117892897 startingPage "3509" @default.
• W2117892897 abstract "Protein arginine methylation has been implicated in signal transduction, nuclear transport and transcription regulation. Protein arginine methyltransferases (PRMTs) mediate the AdoMet-dependent methylation of many proteins, including many RNA binding proteins involved in various aspects of RNA processing and/or transport. Here we describe the crystal structure of the rat PRMT3 catalytic core in complex with reaction product AdoHcy, determined at 2.0 A resolution. The results reveal a two-domain structure: an AdoMet-binding domain and a barrel-like domain. The AdoMet-binding domain is a compact version of the consensus AdoMet-dependent methyltransferase fold. The active site is situated in a cone-shaped pocket between the two domains. The residues that make up the active site are conserved across the PRMT family, consisting of a double-E loop containing two invariant Glu and one His-Asp proton-relay system. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the PRMT family. In addition, crystal packing and solution behavior suggest dimer formation of the PRMT3 core." @default.
• W2117892897 created "2016-06-24" @default.
• W2117892897 creator A5028895511 @default.
• W2117892897 creator A5048679935 @default.
• W2117892897 creator A5050803462 @default.
• W2117892897 date "2000-07-17" @default.
• W2117892897 modified "2023-10-10" @default.
• W2117892897 title "Crystal structure of the conserved core of protein arginine methyltransferase PRMT3" @default.
• W2117892897 cites W1492953040 @default.
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• W2117892897 doi "https://doi.org/10.1093/emboj/19.14.3509" @default.
• W2117892897 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/313989" @default.
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