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. Author manuscript; available in PMC: 2013 Feb 20.
Published in final edited form as: J Mol Biol. 2011 Jul 29;412(4):601–618. doi: 10.1016/j.jmb.2011.07.046

Table 2. Dissociation constants for the binding of TβR-I 7– 91 variants to TGF-β3 in the presence of a near-saturating concentration of TβR-II (2 μM).

Analyte Saturating receptor Kd (μM) Rmax (RU)
TβR-II ED None 0.52 ±0.04 445 ± 19
TβR-I 7–91 None ND ND
TβR-I 7–91 2 μM TβR-II ED 0.31 ±0.02 536 ± 28
P55G TβR-I 7–91 2 μM TβR-II ED ND ND
R58A TβR-I 7–91 2 μM TβR-II ED 20.2±2.2 750 ±38
P59G TβR-I 7–91 2 μM TβR-II ED ND ND
P64A TβR-I 7–91 2 μM TβR-II ED 0.30 ±0.03 362 ± 23

All Kd values, except that for R58A TβR-I, were determined by fitting the observed concentration-dependent maximal response to derive both Kd and Rmax; for R58A TβR-I, Kd was fitted, but Rmax was fixed at the same value obtained for TβR-II binding over the same surface.

ND, not determined due to the minimal response observed.