CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations
J. Clin. Invest. John W. Scott, et al. 113:274 doi:10.1172/JCI19874 [Go to this article.]

Figure 5
(a and b) Binding of ATP by GST fusions of the isolated CBS domain pair (residues 112–232) (a) and full-length IMPDH2 (residues 1–514) (b). (c) Activity of full-length IMPDH2 as a function of ATP concentration. Results were obtained for both the WT sequence and an R224P mutation. Data in a and b were fitted to a single-site binding model as for Figure 1. Data in c were fitted to the model: activity = basal + {[(stimulation × basal) – basal] × [ATP]^h}/(A_0.5^h + [ATP]^h).