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Article

The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain.

Proceedings of the National Academy of Sciences of the United States of America - 23 Jul 2024

van Vlimmeren Anne E, Voleti Rashmi, Chartier Cassandra A, Jiang Ziyuan, Karandur Deepti, Humphries Preston A, Lo Wan-Lin, Shah Neel H

Abstract excerpt

Mutations in the tyrosine phosphatase Src homology-2 domain-containing protein tyrosine phosphatase-2 (SHP2) are associated with a variety of human diseases. Most mutations in SHP2 increase its basal catalytic activity by disrupting autoinhibitory interactions between its phosphatase domain and N-terminal SH2 (phosphotyrosine recognition) domain. By contrast, some disease-associated mutations located in the...

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PMID: 39012820
DOI: 10.1073/pnas.2407159121
PMCID: PMC11287265

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