Discovery of highly potent Src SH2 binders: structure-activity studies and X-ray structures.

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Deprez P, Baholet I, Burlet S, Lange G, Amengual R, Schoot B, Vermond A, Mandine E, Lesuisse D

Discovery of highly potent Src SH2 binders: structure-activity studies and X-ray structures.

Bioorg Med Chem Lett. 2002 May 6;12(9):1291-4.

PubMed ID

11965373 [ View in PubMed

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Abstract

Optimization of the hydrophobic moiety of caprolactam/thiazepinone based compounds led to the identification of potent Src SH2 binders in two different series incorporating a phosphotyrosine group (RU 81843) or a phosphobenzoic group (RU 79181). The X-ray co-structures with the Src SH2 domain revealed different binding modes for RU 81843 and RU 79181, and an excellent fit between RU81843 and the Src SH2 protein thus explaining its high potency (9 nM, 15-fold more potent than pYEEI reference peptide).

DrugBank Data that Cites this Article

Binding Properties

Drug	Target	Property	Measurement	pH	Temperature (°C)
Paratoulene phosphate	Proto-oncogene tyrosine-protein kinase Src	IC 50 (nM)	9	N/A	N/A	Details