Fig. 3: Small molecules stabilize a pre-existing lowly populated 53BP1TT homodimer. | Nature Communications

Fig. 3: Small molecules stabilize a pre-existing lowly populated 53BP1TT homodimer.

From: An autoinhibited state of 53BP1 revealed by small molecule antagonists and protein engineering

Fig. 3: Small molecules stabilize a pre-existing lowly populated 53BP1TT homodimer.The alternative text for this image may have been generated using AI.

a Key inter-53BP1TT contacts in the structure of 53BP1TT-UNC3474 complex. Hydrogen bonds and salt bridges are represented by yellow dashed lines. b Structural overlay of wild-type 53BP1TT and mutant 53BP1TT-PN in which E1549 and D1550 are replaced by a proline and an asparagine, respectively. c NMR spectroscopy-monitored titration of 15N-labeled 53BP1TT-PN with non-labeled H4KC20me2 and p53K382me2 peptides and small molecule UNC1078. Shown in different colors are the overlaid 1H-15N HSQC spectra of 53BP1TT-PN recorded without (black) and with increasing amounts of added compounds, up to fourfold molar excess (red). d Same as c but for the titration of 53BP1TT-PN with small molecules UNC2170, UNC2991, and UNC3474.

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