Fig. 1

The crystal structure of ATAD2 bromodomain (PDB: 6CPS)

Fig. 2

(a) The ATAD2 bromodomain formed gelatinous precipitates. The left tube contains ATAD2 bromodomain solution; the right tube contains buffer solution as a control. (b) The aggregation of ATAD2 bromodomain detected by native-PAGE: Swimlanes 1~5 correspond to 0.025 mmol/L, 0.05 mmol/L, 0.1 mmol/L, 0.25 mmol/L and 0.5 mmol/L of ATAD2 bromodomain in the loading samples, respectively

Fig. 3

(a) 1H- 15N HSQC spectra of ATAD2 bromodomain: The NMR spectrum of the initial ATAD2 bromodomain sample (blue), the NMR spectrum of the sample incubated at 25 ℃ for 8 h (red); (b) The representative NMR signals of ATAD2 bromodomain over time; (c) The intensities of representative NMR signals of ATAD2 bromodomain over time

Fig. 4

(a) CD spectra of ATAD2 bromodomain (BRD) at different concentrations; (b) The percentages of various secondary structures of ATAD2 bromodomain at different concentrations gained from the CD spectra

Fig. 5

(a) 1H NMR spectra of ATAD2 bromodomain incubated at different temperatures. Initial state (blue), incubation state for 8 h (red); (b) The CD spectra of ATAD2 bromodomain at different pH; (c) The CD spectra of ATAD2 bromodomain at different salt concentrations

Fig. 6

(a) 1H- 15N HSQC spectra of C1101A mutant: The initial sample state (blue), the sample incubated at 25 ℃ for 8 h (red); (b) 1H- 15N HSQC spectra of C1057A/C1079A/C1101A mutant: The initial protein sample (blue), the sample incubated at 25 ℃ for 8 h (red); (c) The average signal intensities of 30 NMR resonances of wild-type ATAD2 bromodomain, C1101A mutant and C1057A/C1079A/C1101A mutant over time; (d) The superposition of the initial 1H-15N HSQC spectra of ATAD2 bromodomain wild-type (red) and C1057A/C1079A/C1101A mutant (blue)