Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family.

摘要: Summary The Snf1/AMPK kinases are intracellular energy sensors, and the AMPK pathway has been implicated in a variety of metabolic human disorders. Here we report crystal structure kinase domain from yeast Snf1, revealing bilobe fold with greatest homology to cyclin-dependant kinase-2. Unexpectedly, also reveals novel homodimer that show forms solution, as demonstrated by equilibrium sedimentation, cells, shown coimmunoprecipitation differentially tagged intact Snf1. A mapping sequence conservation suggests dimer formation is conserved feature kinases. conformation αC helix, burial activation segment substrate binding site within dimer, it represents an inactive form kinase. Taken together, these studies suggest another layer regulation family, avenue for development AMPK-specific activating compounds.