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. Author manuscript; available in PMC: 2021 Nov 30.
Published in final edited form as: Curr Protoc Chem Biol. 2019 Sep;11(3):e72. doi: 10.1002/cpch.72

Figure 1. Mechanism of ATP acyl phosphate probe binding.

Figure 1.

The probe ATP moiety enters the active kinase ATP-binding domain and where the acyl phosphate group is positioned in proximity to a conserved lysine residue. The lysine residue reacts with the probe to release ATP, which results in covalent modification of the kinase with a desthiobiotin reporter-tag to permit further subsequent analyses. Pre-treatment of cell lysates with inhibitor to inactivate proteins results in blockade of probe labeling.