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. Author manuscript; available in PMC: 2017 Jan 15.
Published in final edited form as: ACS Chem Biol. 2015 Nov 6;11(1):121–131. doi: 10.1021/acschembio.5b00847

Figure 1.

Figure 1

SNAPtag-based bivalent inhibitors of protein kinases containing a pan-kinase inhibitor tethered to an antibody mimetic. (Top panel) A promiscuous ATP-competitive inhibitor (blue star) blocks the activity of the majority of the kinome (cellular kinase targets are shown as bean-shaped objects and shading represents inhibition of kinase catalytic activity). Non-kinase targets are represented as black shapes. (Middle panel) An intracellular antibody-SNAPtag fusion (SNAPtag is shown in teal and the antibody mimetic is shown in orange) selectively interacts with its kinase target (shown in grey) but does not block catalytic activity. (Bottom panel) A bivalent inhibitor containing a non-selective ATP-competitive inhibitor and an antibody mimetic selectively interacts with its kinase target and blocks catalytic activity.