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. 2013 Jan 24;8(1):e54569. doi: 10.1371/journal.pone.0054569

Figure 3. CSK SH3 and SH2 domains are involved in the association with LYP.

Figure 3

A , Schematic representation of the NMR structure of the Pro rich motif P1 of Pep (orange) bound to the SH3 domain of CSK (blue) (PDB code 1JEG). P1 resid ues are numbered according to the LYP sequence (613IPPPLPVRTPESFIVVEE630). Arg620 is involved in intermolecular polar contacts with Asp27 and Gln26 of CSK; hydrogen bonds are shown by dashed lines. In addition, Arg620 could establish an intramolecular hydrogen bond with Ser624. B, Jurkat cells were electroporated with HA-CSK wild type and several mutants of CSK SH3 domain along myc-LYPR as indicated. Interaction was detected by IB after LYP IP. C, Several HA-CSK mutants in the SH3 and SH2 domains were tested for interaction with myc-LYP-RDA. Jurkat cells were left untreated or treated with PV and LYP was immunoprecipitated from cell lysates. CSK interaction was detected by IB with specific anti-HA antibody. D, Activation of a luciferase reporter gene driven by the IL-2 minimal promoter in Jurkat cells cotransfected with different CSK plasmids, as indicated. The insert shows the IB of the CSK proteins expressed.