Above, the open-state protein of SHP2(SHP2*) was constructed from SHP1, and the allosteric process of SHP2 was investigated by coarse-graining and NRI-MD modeling.
Here, we develop covalent inhibitors that inactivate protein tyrosine phosphatases (PTPs) via electrophilic modification of functional tyrosines.
Src homology 2-domain-containing tyrosine phosphatase 2 (SHP2) is a non-receptor protein tyrosine phosphatase that is widely expressed in a variety of cells and regulates the immune response of T cells through the PD-1 pathway.
We have determined the heterogeneous structural ensemble of the tandem SH2 domains of the protein tyrosine phosphatase SHP2 in agreement with experimental data from small-angle X-ray scattering and NMR residual dipolar couplings in solution.
Development of benzimidazole-based salicylic acid derivatives as novel fluorophores:Identification of the representative benzimidazole-based salicylic acid 5q with excellent SHP1 inhibition and obvious fluorescence specificity for Fe3+.