This model is colored to showcase different properties of the OX40 Receptor (yellow-green) active binding pocket when bound by a OX40 Ligand (three shades of blue). The pocket is bound by Sulfate ions (purple). The first monomer of the trimer complex visualizes the aromatic (cyan) and charged (light green) residues. The second monomer visualizes the hydrophobic residues (red), and the third monomer the positive (blue) residues. Created from PDB ID: 2hey
OX40 is a T cell costimulator activated by OX40L. Blockade of the OX40L-OX40 interaction has ameliorative effects in animal models of T cell pathologies. These structures show that OX40L is an unusually small member of the tumor necrosis factor superfamily (TNFSF). The arrangement of the OX40L protomers forming the functional trimer is atypical and differs from that of other members by a 15 degrees rotation of each protomer with respect to the trimer axis, resulting in an open assembly. Site-directed changes of the interfacial residues of OX40L suggest this interface lacks a single “hot spot” and that instead, binding energy is dispersed over at least two distinct areas. These structures demonstrate the structural plasticity of TNFSF members and their interactions with receptors.
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