Lck (p56lck), a member of the Src family of non-receptor tyrosine protein kinases, is expressed predominantly in T cells. Lck function is critical both for T cell development in the thymus and activation of mature T cells in the periphery by antigen. The activity of Lck is regulated by phosphorylation of two conserved tyrosine residues, Tyr-505 (equivalent to Tyr-529 in c-Src) and Tyr-394 (equivalent to Tyr-418 in c-Src). Tyr-505 is located near the carboxyl terminus of Lck and, when phosphorylated, associates intramolecularly with the SH2 domain in the amino-terminal half of the protein. This helps stabilize Lck in a conformation that, biologically, is relatively inactive. In the absence of phosphorylation at Tyr-505, intramolecular binding of the carboxyl terminus to the SH2 domain does not occur, and Lck exhibits increased activity in vivo.
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