Title : 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.

Pub. Date : 2022 Apr 27

PMID : 35563185






2 Functional Relationships(s)
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1 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. Phosphotyrosine protein tyrosine phosphatase non-receptor type 11 Homo sapiens
2 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. Phosphotyrosine protein tyrosine phosphatase non-receptor type 11 Homo sapiens