2HEV
Crystal structure of the complex between OX40L and OX40
Summary for 2HEV
| Entry DOI | 10.2210/pdb2hev/pdb |
| Related | 2HEW 2HEY |
| Descriptor | Tumor necrosis factor ligand superfamily member 4, Tumor necrosis factor receptor superfamily member 4, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | cytokine, receptor-ligand complex, tnfsf, tnfrsf |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 32109.21 |
| Authors | Hymowitz, S.G.,Compaan, D.M. (deposition date: 2006-06-22, release date: 2006-08-29, Last modification date: 2024-10-30) |
| Primary citation | Compaan, D.M.,Hymowitz, S.G. The Crystal Structure of the Costimulatory OX40-OX40L Complex. Structure, 14:1321-1330, 2006 Cited by PubMed Abstract: 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. In order to better understand the interaction between OX40 and OX40L, we have determined the crystal structure of murine OX40L and of the human OX40-OX40L complex at 1.45 and 2.4 A, respectively. 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. PubMed: 16905106DOI: 10.1016/j.str.2006.06.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.41 Å) |
Structure validation
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