2HEV: Crystal Structure Of The Complex Between Ox40l And Ox40

Citation:
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.
PDB ID: 2HEVDownload
MMDB ID: 41041
PDB Deposition Date: 2006/6/22
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.41  Å
Source Organism:
Similar Structures:
Biological Unit for 2HEV: hexameric; determined by author
Molecular Components in 2HEV
Label Count Molecule
Proteins (6 molecules)
3
Tumor Necrosis Factor Ligand Superfamily Member 4(Gene symbol: TNFSF4)
Molecule annotation
3
Tumor Necrosis Factor Receptor Superfamily Member 4(Gene symbol: TNFRSF4)
Molecule annotation
Chemicals (6 molecules)
1
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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