Fig. 2: Organization of anti-parallel dimers in TNFR superfamily. | Cell Death & Differentiation

Fig. 2: Organization of anti-parallel dimers in TNFR superfamily.

From: CD95/Fas stoichiometry in future precision medicine

Fig. 2: Organization of anti-parallel dimers in TNFR superfamily.The alternative text for this image may have been generated using AI.

A CD95 interactions. Left panel. Solvent accessible surface of the AlphaFold model of the CRD domains of CD95. Color shades correspond to the surface involved exclusively in the dimeric (cyan) or in the ligand binding (salmon) interactions, or shared by both (yellow). The same monomer is shown binding the trimeric ligand (center panel) and the other monomer in the anti-parallel dimer (right panel). The bottom representations in the center and right panels are rotated 90 degrees with respect to the upper representation. B Dimer of CD95 compared to those of DcR3 and TNFR1. First and second rows show receptor dimeric interactions where only one protomer is shown as solvent accessible surface. From left to right CD95 (AlphaFold Multimer prediction), DcR3 (PDB:4MSV), TNFR1 parallel (PDB:1FT4) and anti-parallel (PDB:1EXT) dimers. Third and fourth rows show the corresponding monomer interacting with its ligand. From left to right, CD95-CD95L (AlphaFold Multimer prediction), DcR3-CD95L (PDB:4MSV), and TNFR1-TNFβ (PDB:1TNR). Unlike the lattice contacts observed in anti-parallel TNFR1 (PDB:1EXT) structure and the predicted CD95 anti-parallel dimer, ligand binding domains in the anti-parallel DcR3 or parallel TNFR1 homodimers (PDB:1TNR) involve opposing faces.

Back to article page