SandboxPKA: Difference between revisions
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• '''Protein-binding pocket''': lamina-B domain | • '''Protein-binding pocket''': lamina-B domain | ||
The unactivated conformation ("DGF out") is due to Phe (in the DGF triad) is oriented near the ATP-binding pocket. When Tyr 412 is phosphorylated, “DFG-in” conformation buries the Phe away from the ATP-binding pocket and the A-loop extends over the C terminus of the catalytic domain). The protein can be considered to be in equilibrium among these conformations, with a shift to the activated form upon phosphorylation. <scene name='Dasatinib/Mtot/2'> | The unactivated conformation ("DGF out") is due to Phe (in the DGF triad) is oriented near the ATP-binding pocket. When Tyr 412 is phosphorylated, “DFG-in” conformation buries the Phe away from the ATP-binding pocket and the A-loop extends over the C terminus of the catalytic domain). The protein can be considered to be in equilibrium among these conformations, with a shift to the activated form upon phosphorylation.<scene name='Dasatinib/Mtot/2'>(Morphs of the movement)</scene> | ||
</StructureSection> | </StructureSection> | ||
