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. 2011 Sep 20;6(9):e24655. doi: 10.1371/journal.pone.0024655

Figure 4. Quantitative analysis of the interaction between ARTS CTD and Bir3.

Figure 4

A: Binding of ARTS CTD to Bir3. Bir3 was titrated into fluorescein- labeled ARTS CTD 248–274 (purple) resulting in K d = 8.0±0.7 µM. Titration of Bir3 in the presence of 2 mM DTT resulted in no significant binding (green). B and C: NMR TOCSY spectra of free ARTS CTD (red) and bir3 – bound ARTS CTD (green) show backbone amide chemical shift deviations upon binding. B: Finger print resonances and C: enlargement. D: NMR mapping of the ARTS residues that mediate its binding to Bir3. Shown are the chemical shift changes of ARTS CTD upon interaction with Bir3. The interacting ARTS residues are within the nine C-terminal residues. The largest changes are displayed by residues E267, H268, Q269, C273 and H274.