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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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A) The concentration of bound ZAP-70 as a function of the relative concentration of active kinase (E) to phosphatase (F) for six cytoplasmic CAR domains. These domains include the wild-type -chain (blue), chains containing 3 copies of the low affinity ITAM from FCRI- (green) and FCRI- (red), a single high affinity -chain ITAM (orange), and chains containing a single copy of the low affinity ITAM from FCRI- (magenta) and FCRI- (grey). B-C) Illustrates the and for all CARs shown in panel A. Most CARs are developed based on the wild-type -chain but this construct, although having a large has an undesirably large potency (low ). Novel CARs containing multiple low affinity ITAMs (e.g. (FCRI-)x3, (FCRI-)x3) have the desirably low potency (large ) while maintaining the desirably large .

Inline graphic — A) The concentration of bound ZAP-70 as a function of the relative concentration of active kinase (E) to phosphatase (F) for six cytoplasmic CAR domains. These domains include the wild-type -chain (blue), chains containing 3 copies of the low affinity ITAM from FCRI- (green) and FCRI- (red), a single high affinity -chain ITAM (orange), and chains containing a single copy of the low affinity ITAM from FCRI- (magenta) and FCRI- (grey). B-C) Illustrates the and for all CARs shown in panel A. Most CARs are developed based on the wild-type -chain but this construct, although having a large has an undesirably large potency (low ). Novel CARs containing multiple low affinity ITAMs (e.g. (FCRI-)x3, (FCRI-)x3) have the desirably low potency (large ) while maintaining the desirably large .