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. 2015 Nov;35:116–125. doi: 10.1016/j.dnarep.2015.10.002

Fig. 4.

Fig. 4

Aprataxin phosphopeptide interactions.

(A) Selected chemical shifts from 1H [36] -SOFAST-HMQC spectra (22 °C) of 92 μM aprataxin FHA domain, free (black) and in complex in a 1:4 ratio with XRCC1 peptides YAGSpTDENTDSEEHQ (red), YAGpSpTDENTDSEEHQ (green), YAGpSpTDENpTDSEEHQ (dark blue) and YAGSTDENpTDSEEHQ (cyan). Free and the final bound chemical shift positions are connected by black lines. (B) Predicted interactions between aprataxin and XRCC1 peptides phosphorylated on the core-site (yellow sphere) and subsidiary site (green sphere). The FHA trace is colored on a blue to red scale to indicate the degree of chemical shift movements in 1H [36] -SOFAST-HMQC titrations.