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. 2020 Oct 31;11(3):750–762. doi: 10.1016/j.apsb.2020.10.021

Figure 1.

Figure 1

The structural and allosteric regulation mechanism of Src homology phosphotyrosyl phosphatase 2 (SHP2). (A) The secondary structure of SHP2. SHP2 is a protein tyrosine phosphatase with 593 amino acids, containing N-Src homology 2 (SH2) domain (residues 3–104, green), C-SH2 domain (residues 112–216, purple), protein tyrosine phosphatase (PTP) catalytic domain (residues 221–525, orange), and C-terminal tail (residues 526–593, light blue) with two phosphorylation sites at Tyr542 and Tyr580 (yellow). (B) The “molecular switch” allosteric mechanism of SHP2. SHP2 toggles between the auto-inhibited (left) and allosterically activated (right) conformations. Upon binding with a phosphotyrosyl peptide or oncogenic mutations of PTPN11, SHP2 is dramatically activated along with enhanced enzyme activity.