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. 2016 Sep 19;5:e19058. doi: 10.7554/eLife.19058

Table 1.

Sedimentation equilibrium analytical ultracentrifugation of Sdk fragments. KD = dissociation constant. KI = isodesmic constant. The KI/KD ratio is given when it is less than two, indicating the presence of non-specific binding.

DOI: http://dx.doi.org/10.7554/eLife.19058.003

Protein Oligomeric state Dimerization KD (μM, n=2)
Sdk1
Ig1–4 Dimer 10.5 ± 1.1
Ig1–5 Dimer 4.6 ± 0.06
Ig1–6 Dimer 2.3 ± 0.39
Ig1–2 dimer interface mutations
Ig1–4 N22R Monomer N/A
Ig1–4 K133E Weak non-specific dimer 204 ± 38.9 (KI/K = 1.24)
Ig1–4 L29M/E168D Dimer 4.26 ± 0.50
Ig1–6 N22R Monomer 650 ± 66 (KI/K= 1.05)
Ig3–4 dimer interface mutation
Ig1–4 N253E Dimer 15.5 ± 1.64
Sdk2
Ig1–4 Dimer 2.2 ± 0.4
Ig1–5 Dimer 0.73 ± 0.036
Ig1–6 Dimer 0.44 ± 0.012
Ig1–2 dimer interface mutations
Ig1–4 H18R/N22S Monomer N/A
Ig1–4 N22S Monomer N/A
Ig1–4 N22R Monomer N/A
Ig1–6 H18R/N22S Monomer N/A
Ig3–4 dimer interface mutation
Ig1–4 N253E Dimer 18.9 ± 0.95
Chimera
Sdk2Ig1–2/Sdk1Ig3–4 Dimer 3.92 ± 0.17