M. Anselmi

Atomistic ensemble of active SHP2 phosphatase

The paper presents an atomistic ensemble of the constitutively active SHP2E76K phosphatase using molecular dynamics simulations and SAXS data.

Revealing allostery in PTPN11 SH2 domains from MD simulations

The paper uses MD simulations and PCA to analyze SH2 domain conformations, revealing differences in dynamics between N-SH2 and C-SH2 domains that suggest distinct functional roles.

The loops of the N-SH2 binding cleft do not serve as allosteric switch in SHP2 activation

This study challenges the 'allosteric switch' model of SHP2 activation by showing that N-SH2 binding cleft opening has minimal impact on activation, while central β-sheet opening is more significant.

An allosteric interaction controls the activation mechanism of SHP2 tyrosine phosphatase

This study identifies an allosteric interaction that controls SHP2 activation by stabilizing the N-SH2 domain, revealing how ligand binding influences its conformation and activity.

Structural Determinants of Phosphopeptide Binding to the N-Terminal Src Homology 2 Domain of the SHP2 Phosphatase

This study uses molecular dynamics simulations to analyze the structural determinants of phosphopeptide binding to the N-SH2 domain of SHP2, identifying key residues and interactions that influence binding affinity and specificity.