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Overview
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Background
The strong conservation of the kinase domain among kinome members allows the identification of key amino acids required for the activity of these enzymes. Mutations of one or two conserved lysine residues in the ATP-binding pocket and/or the substrate binding pocket completely abolish the activity of these kinases but do not interfere with substrate recognition or binding to other proteins. Thus, kinase proteins can be modified to generate kinase-dead mutants that are not enzymatically active but have a dominant-negative effect in sequestering the activity of the substrate/interactor, resulting in a loss of function phenotype. The dominant negative effects of kinase-death variants are mediated through interactions between the inactive variant and the effector protein.
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- Properties
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Overview