Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain–modulated complex formation
Copyright policy )Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain–modulated complex formation
Structural analysis of a phosphatase-kinase complex defines a role for the PDZ domain in regulating kinase inactivation.
- University of Queensland Australia
- University of Queensland Australia
- Academia Sinica Taiwan
- National Taiwan University of Arts Taiwan
- Taipei Medical University Taiwan
Biochemistry & Molecular Biology, Spectrometry, Mass, Electrospray Ionization, 1303 Biochemistry, PDZ Domains, Antineoplastic Agents, Crystallography, X-Ray, Neopterin, Mass Spectrometry, Substrate Specificity, 1307 Cell Biology, Mitogen-Activated Protein Kinase 12, Allosteric Regulation, 1312 Molecular Biology, Humans, Trypsin, Cloning, Molecular, Phosphorylation, Glutathione Transferase, Protein Tyrosine Phosphatase, Non-Receptor Type 3, 500, Cell Biology, Cross-Linking Reagents, Drug Design, Mutagenesis, Site-Directed, Peptides, Protein Binding
Biochemistry & Molecular Biology, Spectrometry, Mass, Electrospray Ionization, 1303 Biochemistry, PDZ Domains, Antineoplastic Agents, Crystallography, X-Ray, Neopterin, Mass Spectrometry, Substrate Specificity, 1307 Cell Biology, Mitogen-Activated Protein Kinase 12, Allosteric Regulation, 1312 Molecular Biology, Humans, Trypsin, Cloning, Molecular, Phosphorylation, Glutathione Transferase, Protein Tyrosine Phosphatase, Non-Receptor Type 3, 500, Cell Biology, Cross-Linking Reagents, Drug Design, Mutagenesis, Site-Directed, Peptides, Protein Binding
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