期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 36, 页码 10634-10638出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201604058
关键词
ADP-ribosylation; peptides; posttranslational modifications; proteins; solid-phase synthesis
资金
- Marie Curie Intra-European Fellowship for career development (MitoMAR, FP7-PEOPLE-IEF) [627676]
- Netherlands Organization for Scientific Research (NWO)
Mono-ADP-ribosylation is a dynamic posttranslational modification (PTM) with important roles in signaling. Mammalian proteins that recognize or hydrolyze mono-ADP-ribosylated proteins have been described. We report the synthesis of ADP-ribosylated peptides from the proteins histone H2B, RhoA and, HNP-1. An innovative procedure was applied that makes use of pre-phosphorylated amino acid building blocks. Binding assays revealed that the macrodomains of human MacroD2 and TARG1 exhibit distinct specificities for the different ADP-ribosylated peptides, thus showing that the sequence surrounding ADP-ribosylated residues affects the substrate selectivity of macrodomains.
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