Article

Phosphatase SHP2 pathogenic mutations enhance activity by altering conformational sampling

2025-12-14

Abstract excerpt

SH2 domains are critical mediators of cellular signaling, although the molecular mechanisms by which they bind their phosphopeptide ligands remain incompletely understood. We investigate the atomic mechanisms underlying both healthy regulation and dysregulation of the human protein tyrosine phosphatase SHP2, a key regulator of cellular signaling. While most pathogenic mutations cluster near the PTP/N-SH2 interface...

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Literature Corpus work: 1f5593a7-2cda-5d6c-b290-99cebbc3a8ea
DOI: 10.64898/2025.12.12.694068

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