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. 2011 Jul 18;108(31):12663-12668. doi: 10.1073/pnas.1100758108

Table 1.

Analysis of X4-Cernunnos interactions by calorimetry

Cernunnos * Xrcc4 * Kd (μM) Commentary Reference
WT1–224 WT1–203 3.9 ± 0.2 29
WT1–224 WT1–157 4.1 ± 0.2 X4(1-157) central coiled-coil 60 Å shorter than X4(1–203) this study
WT1–224 E55R1–157 no interaction in helix α1, salt bridge with R64C this study
WT1–224 D58R1–157 no interaction in helix α1, close to E55C and R64C this study
WT1–224 M61R1–157 no interaction in loop α1–α2, in contact with P116C and L115C this study
WT1–224 E62R1–157 3.8 ± 0.2 in helix α2, salt bridge with K65X this study
WT1–224 K65E1–157 > 40 in helix α2, salt bridge with E111C and E62X this study
WT1–224 E69R1–157 5.0 ± 0.2 in helix α2, salt bridge with K99X and hydrogen bond with Y84X this study
WT1–224 F106E1–157 no interaction in strand β7, in contact with L65C, A67C, F72C, and L112C this study
WT1–224 F106A1–157 > 40 see above this study
WT1–224 F106Y1–157 > 40 see above this study
E111K1–224 WT1–157 6.9 ± 0.2 in strand β6, salt bridge with K65X this study
R64E1–224 WT1–203 no interaction in loop α2–α3, salt-bridge with E55X and close to D58X 29
L65D1–224 WT1–203 > 80 in loop α2–α3, in contact with F106X 29
L115D1-224 WT1–203 no interaction in strand β7, in contact with F106XM61X, M59X and L108X 29

*The limits of the constructs used for X4 and Cernunnos are indicated in superscript.