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Conformational transitions in protein kinases are crucial for the biological function of these enzymes. Here, we characterize and assess conformational equilibria of the activation loop and the effect of small… Click to show full abstract
Conformational transitions in protein kinases are crucial for the biological function of these enzymes. Here, we characterize and assess conformational equilibria of the activation loop and the effect of small molecule inhibitors in the MAP kinase p38α. Our work experimentally revealed the existence of a two-state equilibrium for p38α while the addition of inhibitors shifts the equilibrium between these two states.
Keywords:
equilibria activation;
kinase p38;
conformational equilibria;
activation loop
Journal Title: Chemical communications
Year Published: 2018
Link to full text (if available)
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Journal Title: Chemical communications
Year Published: 2018
Link to full text (if available)
Share on Social Media: Sign Up to like & get
recommendations!