Abstract
Mapping the Interaction between the Mitogen-activated Protein Kinase p38α and Its Regulatory Phosphatase♦: Structural Basis for the Regulation of the Mitogen-activated Protein (MAP) Kinase p38α by the Dual Specificity Phosphatase 16 MAP Kinase Binding Domain in Solution
Highlights
Brown University in Rhode Island demonstrated that one of these phosphatases, DUSP16, interacts with Mitogen-activated protein kinases (MAPKs) p38␣ in a way different from other dual specificity phosphatases
Mitogen-activated protein kinases (MAPKs) are critical in signal transduction pathways and are important pharmaceutical targets. Their activities are regulated by a number of proteins, including dual specificity phosphatases
By looking at the solution structure of the two proteins using nuclear magnetic resonance and small-angle xray scattering as well as monitoring the binding by isothermal titration calorimetry, the investigators showed that the MAPK binding domain
Summary
Brown University in Rhode Island demonstrated that one of these phosphatases, DUSP16, interacts with MAPK p38␣ in a way different from other dual specificity phosphatases. Mapping the Interaction between the Mitogen-activated Protein Kinase p38␣ and Its Regulatory Phosphataseࡗ
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