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Title 

Sclerotiorin and isochromophilone IV: inhibitors of Grb2-Shc interaction, isolated from Penicillium multicolor F1753

Authors 

Ji Youn NamKwang Hee SonHyae Kyeong KimMi Young HanSung Uk KimJung Do ChoiByoung-Mog Kwon

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2000

Citation 

Journal of Microbiology and Biotechnology, vol. 10, no. 4, pp. 544-546

Keywords 

Grb2Shcsignal transductionantitumor

Abstract 

Grb2 is an important adaptor protein in the mitogenic Ras signaling pathway of receptor tyrosine kinases, and contains one SH2 domain and two SH3 domains. The SH2 domain binds to specific phosphotyrosine motifs on receptors or adaptor proteins such as Shc. The SH2 domain antagonists may lead to blocking of the oncogenic Ras signals and to developing new antitumor agents. In the course of screening SH2 antagonists from natural sources, sclerotiorin (1) and isochromophilone IV (2) were isolated from a strain, Penicillium multicolor F1753, and their structures were established by NMR spectral data. The metabolites significantly inhibited the binding between the Grb2-SH2 domain and phosphopeptide derived from the Shc protein, with IC50 values of 22 μM and 48 μM for (1) and (2), respectively. The compounds are the first non-peptidic inhibitors of the SH2 domain from a natural source.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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