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. Author manuscript; available in PMC: 2008 Jun 23.
Published in final edited form as: Biochemistry. 2007 Feb 13;46(6):1663–1671. doi: 10.1021/bi0617613

Table 1.

Dissociation Constants for Synthetic and Expressed wt bZIP Bound to DNA Sites

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
a

Average values of dissociation constants were obtained from two independent experiments; R values >0.97.

b

Higher-order bandshifts were not included in calculation of dissociation constants (see text and Supporting Information).

c

Saturation protein binding was not achieved in these titrations.

d

The concentration of wt bZIP ranged from 0 to 1000 nM.

e

From ref 17.