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. 2013 Mar 28;9(3):e1003004. doi: 10.1371/journal.pcbi.1003004

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© 2013 Mukhopadhyay et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Inline graphic — A) The concentration of ITAM-bound ZAP-70 as a function of the relative kinase (E) to phosphatase (F) concentration. As expected, when the phosphatase is in excess the -chain is dephosphorylated and ZAP-70 cannot bind whereas when the kinase is in excess the -chain is phosphorylated and ZAP-70 is fully bound. Results are shown for the wild-type -chain (123) and for -chains where the first and second ITAMs are removed, X23 and XX3, respectively. Inset shows normalized curves, highlighting differences in potency () and sensitivity (Hill number), which is a measure of the curve steepness. Each curve is fit to a Hill function to extract estimates of B) the maximum (), C) the potency (), and D) the sensitivity (Hill number). Model and parameter values can be found in Methods.

A) The concentration of ITAM-bound ZAP-70 as a function of the relative kinase (E) to phosphatase (F) concentration. As expected, when the phosphatase is in excess the -chain is dephosphorylated and ZAP-70 cannot bind whereas when the kinase is in excess the -chain is phosphorylated and ZAP-70 is fully bound. Results are shown for the wild-type -chain (123) and for -chains where the first and second ITAMs are removed, X23 and XX3, respectively. Inset shows normalized curves, highlighting differences in potency () and sensitivity (Hill number), which is a measure of the curve steepness. Each curve is fit to a Hill function to extract estimates of B) the maximum (), C) the potency (), and D) the sensitivity (Hill number). Model and parameter values can be found in Methods.