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. 2008 Jul 23;82(19):9657–9667. doi: 10.1128/JVI.00107-08

FIG. 1.

FIG. 1.

In vitro binding between ht-fbr and GST-SF2Nef. (A) In vitro binding reactions utilizing purified proteins from bacteria were performed with PACS-1 ht-fbr and a GST fusion protein. A Western blot to detect bound ht-fbr is shown at the top. Lane 1, GST negative control; lane 2, GST-SF2Nef fusion protein; lane 3, GST-furin tail SDS (dephosphorylated AC); lane 4, GST-furin tail DDD (phosphorylation mimic AC); and lane 5, loading control of 1% of the ht-fbr input. The lower panel is a Western blot with anti-GST. (B) In vitro binding reaction with GST-SF2Nef fusion protein and histidine-tagged Hck SH3 domain (ht-HckSH3). Lane 1, GST negative control; lane 2, GST-SF2Nef fusion protein; and lane 3, loading control of 4% of the ht-HckSH3 input.