Fig. 5

Theoretical modeling and molecular dynamics simulation of the interaction between Tet2 and Stat1. A 3D structure of Tet2 predicted using AlphaFold2. The central structured region is in cartoon representation and rendered in light blue. The intrinsic disorder region is in tube representation and colored in gray. B 3D structure of Stat1 predicted using AlphaFold2. The tail segment has a transparent surface and tube representation; the remaining domains are opaque. C The complex structure (formed by the structured region of Tet2 and the SH2/linker domains plus the tail segment of Stat1) was predicted using AlphaFold-multimer. The region/domains are rendered using the same color code as in (A) and (B). D Enlargement of the interaction interface between Stat1 and Tet2. Tet2 is in light blue transparent surface representation. Three tubes show conformations of a part of the tail segment of Stat1 embedded in the pocket at three simulation times. Two residues (Arg1261/His1386) in stick representation are involved in the interaction between Tet2 and its inhibitor BC339. E Red curve: Root-mean-square deviation (RMSD) of the tail segment embedded in the active pocket as shown in (D); Blue curve: distance between the center of mass of the structured region of Tet2 and that of the SH2 domain of Stat1. The light (deep) color indicates the original (smoothed) data