Nonpeptidic, monocharged, cell permeable ligands for the p56lck SH2 domain

…, JM Ferland, J Gauthier, J Gillard, V Gorys…

Index: Proudfoot; Betageri; Cardozo; Gilmore; Glynn; Hickey; Jakes; Kabcenell; Kirrane; Tibolla; Lukas; Patel; Sharma; Yazdanian; Moss; Beaulieu; Cameron; Ferland; Gauthier; Gillard; Gorys; Poirier; Rancourt; Wernic; Montse Journal of Medicinal Chemistry, 2001 , vol. 44, # 15 p. 2421 - 2431

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Citation Number: 19

Abstract

p56lck is a member of the src family of tyrosine kinases and plays a critical role in the signal transduction events that lead to T cell activation. Ligands for the p56lck SH2 domain have the potential to disrupt the interaction of p56lck with its substrates and derail the signaling cascade that leads to the production of cytokines such as interleukin-2. Starting from the quintuply charged (at physiological pH) phosphorylated tetrapeptide, AcpYEEI, we ...