Summary
PDB 1DQT deposited: 2000-01-05 modified: 2009-02-24
Title THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)
Authors Almo, S.C., Nathenson, S.G., Ostrov, D.A., Schwartz, J.C., Shi, W.
Method X-RAY DIFFRACTION
Structure factors resolution 2.0 rfactor 0.2106 rfree 0.2543
DPI 0.58 theoretical min: 0.20
Citations

The effective regulation of T cell responses is dependent on opposing signals transmitted through two related cell-surface receptors, CD28 and cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). Dimerization of CTLA-4 is required for the formation of high-avidity complexes with B7 ligands and for transmission of signals that attenuate T cell activation. We determined the crystal structure of the extracellular portion of CTLA-4 to 2.0 angstrom resolution. CTLA-4 belongs to the immunoglobulin superfamily and displays a strand topology similar to Valpha domains, with an unusual mode of dimerization that places the B7 binding sites distal to the dimerization interface. This organization allows each CTLA-4 dimer to bind two bivalent B7 molecules and suggests that a periodic arrangement of these components within the immunological synapse may contribute to the regulation of T cell responsiveness.

Science 2000 Oct; 290(5492):816-819 doi:10.1126/science.290.5492.816

Cross References
Database source Identifier Description
PubMed 11052947 SCIEAS
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1DQT/1 1DQT 1 dimer 0 2 3 1935
1DQT/2 1DQT 2 dimer 0 2 2 1884
1DQT/3 1DQT 3 tetramer 0 4 5 3819