Figure 4.

Key interactions between FAM181A^190–205/FAM181B^220–235 and TEAD4. Left panels. The structures of the FAM181A^190–205:TEAD4 (pdb http://bioinformatics.org/firstglance/fgij//fg.htm?mol=6SEN) and YAP^60–100:TEAD4 (pdb http://bioinformatics.org/firstglance/fgij//fg.htm?mol=6GE3 26) complexes have been superimposed. The residues of FAM181A, YAP and TEAD are represented by green, orange and gray sticks, respectively. Right panels. The structures of the FAM181B^220–235:TEAD4 complexes (pdb http://bioinformatics.org/firstglance/fgij//fg.htm?mol=6SEO) and YAP^60–100:TEAD4 (pdb http://bioinformatics.org/firstglance/fgij//fg.htm?mol=6GE3 26) complexes have been superimposed. The residues of FAM181B, YAP and TEAD are represented by magenta, orange and gray sticks, respectively. (a). Hydrophobic core of the Ω‐loop. (b). Residues involved in the stabilization of the hydrophobic core. (c). Salt bridge with Asp272^TEAD4. (d). Hydrogen bonds with Glu263^TEAD4:Tyr429^TEAD4 and position of the conserved proline at the binding interface. The picture was drawn with PyMOL (Schrödinger Inc., Cambridge, Massachusetts)