SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange.

Ítems similars

• SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma.
  per: Rotin, D, et al.
  Publicat: (1992)
• Tyrosine Phosphorylation of the Lyn Src Homology 2 (SH2) Domain Modulates Its Binding Affinity and Specificity
  per: Jin, Lily L., et al.
  Publicat: (2015)
• The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors.
  per: Li, W, et al.
  Publicat: (1992)
• SH3 Domain Tyrosine Phosphorylation – Sites, Role and Evolution
  per: Tatárová, Zuzana, et al.
  Publicat: (2012)
• The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling.
  per: Skolnik, E Y, et al.
  Publicat: (1993)