| First Author | Ostrov DA | Year | 2000 |
| Journal | Science | Volume | 290 |
| Issue | 5492 | Pages | 816-9 |
| PubMed ID | 11052947 | Mgi Jnum | J:65436 |
| Mgi Id | MGI:1926576 | Doi | 10.1126/science.290.5492.816 |
| Citation | Ostrov DA, et al. (2000) Structure of murine CTLA-4 and its role in modulating T cell responsiveness. Science 290(5492):816-9 |
| abstractText | 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. |
