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You notice that some Lck functions are still being performed, although less efficiently. What is the...

You notice that some Lck functions are still being performed, although less efficiently. What is the likely mechanism for this?
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lymphocyte-specific protein tyrosine kinase is an enzyme that is found in the specialized cell of immune system. It is a tyrosine kinase which phosphorylates tyrosine residue of certain protein that are involved in the intracellular signaling pathway of lymphocytes.

When the T cell receptor is engaged by the specific antigen presented by major histocompatibility complex, Lck acts to phosphorylate the intracellular chains of the CD3 and ζ-chains of the T cell receptor complex, allowing another cytoplasmic tyrosine kinase called ZAP-70 to bind to them. Lck then phosphorylates and activates ZAP-70, which in turn phosphorylates another molecule in the signaling cascade

Lck signaling has been proposed as a mechanism of CD4/CD8 commitment. Strong Lck signaling favors the differentiation of DP cells into CD4+ SP cells, while little or no signaling results in CD8+ SP cells. As the amount of Lck signaling is determined by the major histocompatibility complex (MHC) rectrition of the TCR, MHC class I-restricted TCRs bind to CD8, which is associated with low levels of Lck activity, while MHC class II-restricted TCRs bind to CD4, which is associated with about 20-fold higher levels of Lck activity.

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