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  • 1
    ISSN: 0948-5023
    Keywords: Keywords: Immunoglobulin superfamily ; comparative protein structure prediction ; sequence-structure analysis ; molecular model ; solution structure ; model-structure-comparison
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The CD28 and CTLA-4 (CD152) receptors on T cells recognize CD80 and CD86 ligands on antigen presenting cells. These interactions provide and control costimulatory signals required for effective T cell activation. CD28 and CTLA-4 belong to the immunoglobulin superfamily (IgSF) and contain a single extracellular ligand binding domain. The three-dimensional (3D) structure of the binding domain of CTLA-4 was modeled previously using a combination of structure-based sequence comparison, IgSF consensus residue analysis, conformational search, and inverse folding calculations. Recently, the 3D structure of CTLA-4 was determined by NMR. Comparison of the modeled and experimentally determined CTLA-4 structure has made it possible to assess the accuracy of our predictions. We found that the overall accuracy of the model was sound and sufficient for a meaningful application of the model in experimental studies. Major errors in the model are limited to the conformation and position of some loops. Our studies on CTLA-4 provide an example for the opportunities and limitations of comparative protein modeling in the presence of low sequence similarity.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Perspectives in drug discovery and design 2 (1994), S. 221-231 
    ISSN: 1573-9023
    Keywords: CTLA-4 ; B7 ; T-cell costimulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The CD28 and CTLA-4 molecules on T cells and their counterreceptors, B7-1 and B7-2, on antigen-presenting cells constitute an important costimulatory pathway for immune responses to antigen in vitro and in vivo. A primary function of these interactions is to regulate production of T-cell-derived cytokines, including interleukin 2. A soluble form of the CTLA-4 receptor, CTLA4Ig, has been produced which binds B7 with high avidity and functions as a competitive inhibitor of CD28/CTLA-4 interactions. In rodent models, CTLA4Ig inhibits T-dependent antibody responses, blocks organ graft rejection, prevents death from acute graft-versus-host disease, and prevents autoimmune disease. CTLA4Ig has a novel mechanism of action, and also has several attractive features for an immunosuppressive drug, including low toxicity, long serum half-life, and the ability to induce long-lasting antigen-specific immune suppression (tolerance) after therapy. CTLA4Ig thus represents a prototype of a new class of immunosuppressive drugs which function by blocking T-cell costimulation through the CD28 receptor.
    Type of Medium: Electronic Resource
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