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The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain
Mutations in the tyrosine phosphatase SHP2 are associated with a variety of human diseases, including cancer and developmental disorders. Most mutations in SHP2 increase its basal catalytic activity by disrupting auto-inhibitory interactions between its phosphatase domain and N-terminal SH2 (phospho...
| Autores principales: | , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Cold Spring Harbor Laboratory
2023
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10369915/ https://www.ncbi.nlm.nih.gov/pubmed/37502916 http://dx.doi.org/10.1101/2023.07.10.548257 |