期刊
SCIENCE
卷 290, 期 5492, 页码 816-819出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.290.5492.816
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资金
- NCI NIH HHS [CA09173] Funding Source: Medline
- NIAID NIH HHS [AI07289, AI42970] Funding Source: Medline
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 Vor 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.
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