NMR-based discovery of phosphotyrosine mimetics that bind to the Lck SH2 domain.
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.
Hajduk
P J
PJ
Abbott Laboratories, Abbott Park, IL 60064, USA.
Zhou
M M
MM
Fesik
S W
SW
D009682:Magnetic Resonance Spectroscopy; D018716:Molecular Mimicry; D015394:Molecular Structure; D019000:Phosphotyrosine / Q000737:chemistry*; D011485:Protein Binding; D011505:Protein-Tyrosine Kinases / Q000737:chemistry / Q000378:metabolism*; D018909:src Homology Domains
D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases