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- Title
Structure of murine CTLA-4 and its role in modulating T cell responsiveness.
- Authors
Ostrov, D A; Shi, W; Schwartz, J C; Almo, S C; Nathenson, S G
- Abstract
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.
- Publication
Science (New York, N.Y.), 2000, Vol 290, Issue 5492, p816
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.290.5492.816