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...

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Detalles Bibliográficos
Autores principales: van Vlimmeren, Anne E., Voleti, Rashmi, Chartier, Cassandra A., Jiang, Ziyuan, Karandur, Deepti, Shah, Neel H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Article
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

Internet

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

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