Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction

Post-translational protein modification by tyrosine sulfation has an important role in extracellular protein–protein interactions. The protein tyrosine sulfation reaction is catalysed by the Golgi enzyme called the tyrosylprotein sulfotransferase. To date, no crystal structure is available for tyros...

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Bibliographic Details
Published in:	Nature communications Vol. 4; no. 1; p. 1572
Main Authors:	Teramoto, Takamasa, Fujikawa, Yukari, Kawaguchi, Yoshirou, Kurogi, Katsuhisa, Soejima, Masayuki, Adachi, Rumi, Nakanishi, Yuichi, Mishiro-Sato, Emi, Liu, Ming-Cheh, Sakakibara, Yoichi, Suiko, Masahito, Kimura, Makoto, Kakuta, Yoshimitsu
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 2013 Nature Publishing Group
Subjects:	631/45/173 631/45/535 Adenosine Diphosphate - chemistry Adenosine Diphosphate - metabolism Binding Sites Biocatalysis Catalytic Domain Crystallography, X-Ray Humanities and Social Sciences Humans Membrane Proteins - chemistry Membrane Proteins - metabolism Models, Molecular multidisciplinary Mutant Proteins - chemistry Mutant Proteins - metabolism Peptides - chemistry Peptides - metabolism Protein Multimerization Protein Processing, Post-Translational Protein Structure, Secondary Protein-Tyrosine Kinases - chemistry Science Science (multidisciplinary) Static Electricity Structural Homology, Protein Substrate Specificity Sulfates - metabolism Sulfotransferases - chemistry Sulfotransferases - metabolism Tyrosine - chemistry Tyrosine - metabolism
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