Open conformation SHP2

The tyrosine phosphatase SHP2 interconverts between open, active, and closed, inactive, structures to regulate crucial cell signaling pathways. Oncogenic mutations such as E76K shifts the equilibrium towards the open state making SHP2 200 fold more active than WT. In contrast to the closed state of SHP2 that has been well described mainly by crystal structures, the open structure is unknown and possibly adopts a ensemble of states in solution that hampers crystallization. Using homology modeling...
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