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. 2019 Oct 9;294(46):17383–17394. doi: 10.1074/jbc.RA119.009589

Figure 2.

Figure 2.

Schematic representation and far UV CD profiles of KIBRA WW domain constructs. A, The constructs used in this study were tandem WW domain (KWWTD), KWWTD variants with single point mutations in the WW1 (P37ATD) and WW2 (P84ATD and I81WTD) domains, individual WW domains (KWW1 or KWW2), and a KWW2 mutant (KWW2-I81W). Sequence-based secondary structure predictions are shown for the KWWTD construct. Two segments in the WW1 domain and a segment in the WW2 domain have β strand propensities (arrows). The rest of the protein is predicted to be disordered (dotted lines). B, far UV CD spectra of isolated WW domain constructs KWW1 (black), KWW2 (red), and KWW2-I81W (brown). C, far UV CD spectra of KWWTD (orange), P84ATD (green), I81WTD (magenta), and P37ATD (black). The P37A mutation decreases the signal at 230 nm. CD data were collected in 10 mm sodium phosphate, pH 6.8 or 8.0.