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. 2014 Oct 18;24(1):81–92. doi: 10.1002/pro.2590

Table II.

Summary of NMR Titration Experiments of hCXCR1Ndp Binding to CXCL8 Variants

Complex Buffer conditions Temp CXCL8 conc. Start/end (μM)c Final Peptide Conc. (μM) Molar ratio FB (%) KdM)d
WT + h29mera,b 50 mM Pi, pH 7.0 30°C 90/62 711 1:11.5 87 ± 2 103 ± 12
WT + h29mera,b 50 mM Pi, pH 6.0 30°C 100/80 850 1:10.5 98 ± 1 17 ± 4
WT + h21mera,b 50 mM Pi, 150 NaCl, pH 6.5 25°C 125/20 2660 1:134 79 ± 3 700 ± 90
R26C + h29mer 50 mM Pi, pH 7.0 30°C 150/129 1029 1:11.2 85 ± 3 172 ± 24
1–66 monomer + h29mer 50 mM Pi, pH 6.0 30°C 200/135 1135 1:8.4 >99 <5
V27P/E29P monomer + h29mer 50 mM Pi, pH 7.0 30°C 100/65 777 1:11.9 >99 <5
V27P/E29P monomer + h21mer 50 mM Pi, pH 7.0 30°C 100/72 461 1:6.4 90 ± 3 43 ± 10
V27P/E29P monomer + h21mer 50 mM Pi, 150NaCl, pH 6.5 25°C 100/69 945 1:13.8 88 ± 2 118 ± 14
L25Y/V27R monomer + h21mer 50 mM Pi, pH 7.0 30°C 100/63 506 1:8 77 ± 5 135 ± 25
L25Y/V27R monomer + h21mer 50 mM Pi, 150 NaCl, pH 6.5 25°C 150/62 1176 1:19 72 ± 2 432 ± 25
a

WT dimer dissociation was coupled to receptor peptide binding

b

Kd calculated for the dimer.

c

Concentrations are reported in monomer units.

d

Kd values are averages calculated from a subset of 8–15 residues; Pi, phosphate.