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. 1999 Aug 15;13(16):2087–2097. doi: 10.1101/gad.13.16.2087

Figure 1.

Figure 1

Figure 1

cdr2 and c-Myc interact in vitro. A GST pull-down assay was used to examine the in vitro binding of cdr2 and c-Myc. Immobilized GST fusion proteins were incubated with full–length in vitro translated c-Myc and cdr2. (A) Full–length 35S-labeled c-Myc binds to GST–cdr2 in vitro. c-Myc did not bind to GST alone, and weakly bound to GST–USF, another HLZ protein. GST–Max was used as a positive control. (B) Full–length 35S-labeled cdr2 interacted with a truncated c-Myc fusion protein that contained the HLZ domain (Myc439) and also bound to itself (GST–cdr2). Cdr2 did not bind to GST alone, GST–Max, or Myc353, which lacks the HLZ region. The arrows indicate the size of the full-length 35S-labeled proteins.