The active site of O-GlcNAc transferase imposes constraints on substrate sequence

O-GlcNAcylation is a post-translational modification catalyzed by O-GlcNAc transferase. Here, a high-throughput activity assay combined with mass spectrometric and crystallographic analyses sheds light on the substrate recognition and specificity of O-GlcNAc transferase. O-GlcNAc transferase (OGT) g...

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Veröffentlicht in:	Nature structural & molecular biology 2015-09, Vol.22 (9), p.744-750
Hauptverfasser:	Pathak, Shalini, Alonso, Jana, Schimpl, Marianne, Rafie, Karim, Blair, David E, Borodkin, Vladimir S, Schüttelkopf, Alexander W, Albarbarawi, Osama, van Aalten, Daan M F
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/173 631/45/221 631/535/1266 631/80/458/1524 Binding sites Biochemistry Biological Microscopy Catalytic Domain Crystal structure Crystallography Crystallography, X-Ray Electron transfer Electron transport Glycosylation Humans Life Sciences Mass Spectrometry Membrane Biology Models, Molecular N-Acetylglucosamine N-Acetylglucosaminyltransferases - chemistry N-Acetylglucosaminyltransferases - metabolism O-GlcNAcylation Peptides Post-translation Protein Conformation Protein Structure Proteins Recognition Spectrometry Substrate Specificity Substrates Transferases Translation
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