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. Author manuscript; available in PMC: 2023 Apr 15.
Published in final edited form as: J Mol Biol. 2023 Feb 16;435(8):168010. doi: 10.1016/j.jmb.2023.168010

Figure 3.

Figure 3.

Characterization of SHP2 allostery using Mb13 as a probe for the accessibility of the PTP active site. (a) Cartoon depicting the open-closed equilibrium of SHP2 and binding of Mb13 to the open state but not to the closed state. (b) BLI sensorgrams for the interaction of the full-length, ΔN-SH2 and N-terminally tagged constructs of WT SHP2 with Mb13 immobilized on a sensor tip. The tag consists of His6, Avi-tag and a TEV cleavage sequence. (c) BLI sensorgrams for the interaction of full-length SHP2 mutants with Mb13 immobilized on a sensor tip. (d) BLI sensorgrams for the interaction of the indicated SHP2 constructs with Mb13 in the absence and presence of the tandem pY peptide derived from GAB2. The right bottom panel shows the interaction of SHP2(C459E) in the presence of 300 nM pY peptide.