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. 2011 May 12;286(28):25236–25245. doi: 10.1074/jbc.M110.216333

FIGURE 1.

FIGURE 1.

The tandem WW domains of HYPA have an interdomain chaperoning effect and enhanced interaction with the N-terminal Htt. A, shown are schematic architectures of the N-terminal fragment of Htt18Q (1–171), the N terminus of HYPA (1–423), and the mouse homolog of HYPA, FBP11. The fragment of HYPA also includes a nuclear localization signal (NLS) sequence. B, GST pulldown and Western blotting experiments for the interactions of various WW domains with Htt18Q are shown. The SDS-PAGE with Coomassie staining shows the loading of GST and GST fusion proteins (lower). C, GST shown are pulldown and Western blotting experiments for the interactions of various WW domains with Htt100Q. The Htt100Q protein shows a smear in the gels. D, shown is an overlay plot of the 15N,1H HSQC spectra of 2WW (red), WW1 (cyan), and WW2 (orange). The proteins (∼200 μm) were dissolved in 10 mm sodium phosphate buffer at pH 6.0 for NMR experiments.