title: NMR Spectroscopy to Study MAP Kinase Binding to MAP Kinase Phosphatases.
abstract: NMR spectroscopy and other solution methods are increasingly being used to obtain novel insights into the mechanisms by which MAPK regulatory proteins bind and direct the activity of MAPKs. Here, we describe how interactions between the MAPK p38α and its regulatory proteins are studied using NMR spectroscopy, isothermal titration calorimetry, and small angle X-ray scattering (SAXS).
authors: Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI, 02912, USA. Wolfgang_Peti@brown.edu.|Department of Chemistry, Brown University, Providence, RI, 02912, USA. Wolfgang_Peti@brown.edu.
authors: Wolfgang
authors: W
authors: Peti
authors: Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, 02912, USA.
authors: Rebecca
authors: R
authors: Page
mesh_terms: D000818:Animals; D002151:Calorimetry / Q000379:methods*; D006801:Humans; D048308:Mitogen-Activated Protein Kinase 14 / Q000737:chemistry / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D060066:Protein Interaction Maps; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry / Q000378:metabolism; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D048308:Mitogen-Activated Protein Kinase 14; D017027:Protein Tyrosine Phosphatases
keywords: Chemical shift perturbation (CSP); D2O; Dual specificity phosphatase; Isothermal titration calorimetry (ITC); Isotopically labeled growth media; Mitogen activated protein kinase (MAPK); Nuclear magnetic resonance (NMR) spectroscopy; Protein tyrosine phosphatases; Protein–protein interaction; Small angle X-ray scattering (SAXS); p38α