Table 1.
Kd (10-9 M)a |
||
---|---|---|
binding site | synthetic wt bZIP | expressed wt bZIPb |
WT AP-1 | 13 ± 0.38 | |
AP-1 | 13 ± 0.59e | 4.8 ± 0.12b |
CRE | 12 ± 0.28 | |
C/EBP | 120 ± 16e | 29 ± 3.6b |
XRE1 | 240 ± 18e | |
Arnt E-box | 570 ± 0.69c,e | |
Max E-box | 840 ± 26c | |
HRE | 1400 ± 160c,e | |
Partial | 280 ± 49e | |
AP-1 half | 84 ± 0.01 | 23 ± 8.7b |
C/EBP half | >5000c | >1500c |
Arnt E-box half | >4000c | |
Max E-box Half | no activityd | |
NS | no activityd | no activityd |
Average values of dissociation constants were obtained from two independent experiments; R values >0.97.
Higher-order bandshifts were not included in calculation of dissociation constants (see text and Supporting Information).
Saturation protein binding was not achieved in these titrations.
The concentration of wt bZIP ranged from 0 to 1000 nM.
From ref 17.