NMR-based discovery of phosphotyrosine mimetics that bind to the Lck SH2 domain

P J Hajduk; M M Zhou; S W Fesik

doi:10.1016/s0960-894x(99)00403-5

NMR-based discovery of phosphotyrosine mimetics that bind to the Lck SH2 domain

Bioorg Med Chem Lett. 1999 Aug 16;9(16):2403-6. doi: 10.1016/s0960-894x(99)00403-5.

Authors

P J Hajduk¹, M M Zhou, S W Fesik

Affiliation

¹ Abbott Laboratories, Abbott Park, IL 60064, USA.

PMID: 10476877
DOI: 10.1016/s0960-894x(99)00403-5

Abstract

Using an NMR-based screen, a series of novel phosphotyrosine mimetics were discovered that bind to the SH2 domain of Lck. These compounds may serve as useful leads for the design of nonpeptide inhibitors of SH2 domains with improved bioavailability and metabolic stability compared to the natural ligands that contain phosphotyrosine.

MeSH terms

Magnetic Resonance Spectroscopy
Molecular Mimicry*
Molecular Structure
Phosphotyrosine / chemistry*
Protein Binding
Protein-Tyrosine Kinases / chemistry
Protein-Tyrosine Kinases / metabolism*
src Homology Domains*

Substances

Phosphotyrosine
Protein-Tyrosine Kinases