Intramolecular Interaction with the E6 Region Stabilizes the Closed Conformation of the N-SH2 Domain and Concurs with the Self-Inhibitory Docking in Downregulating the Activity of the SHP2 Tyrosine Phosphatase: A Molecular Dynamics Study

The localization and activity of the SHP2 tyrosine phosphatase across different cellular compartments to the target substrates are steered by the binding of phosphotyrosine (pY) peptides to the tandem SH2 domains. The most N-terminal domain (N-SH2) can also keep the enzyme inactive by intramolecular...

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Detalles Bibliográficos
Autor principal: Bellacchio, Emanuele
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9105505/
https://www.ncbi.nlm.nih.gov/pubmed/35563185
http://dx.doi.org/10.3390/ijms23094794

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9105505/
https://www.ncbi.nlm.nih.gov/pubmed/35563185
http://dx.doi.org/10.3390/ijms23094794

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