배초향으로부터 Grb2-Shc domain 결합저해 물질의 분리

Isolation of Grb2-Shc Domain Binding Inhibition Component from Agastache rugosa

SH2 domains and their associated catalytic or noncatalytic proteins constitute critical signal transduction targets for drug discovery. Grb2 associates with phosphotyrosine sites of the activated receptors or Shc via their SH2 domain to link receptor tyrosine kinases to ras signalling. Blocking of the Grb2-Shc complex may be to intervene the oncogenic signal transduction pathways and to develop a new antitumor drug. In the search for blockers of Grb2 SH2-Shc interaction, Lutein, a family of carotenoids, was isolated from the extract of the leaf of Agastache rugosa O. Kuntze as SH2 domain antagonists. The $IC_{50}$ of Lutein against Grb2-Shc binding was $6.8\;{\mu}M$.