Summary
B7-1 and B7-2 are glycoproteins expressed on antigen presenting cells. The binding of these molecules to the T-cell homodimers, CD28 and CTLA-4, generate ‘costimulatory’ and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-l), solved to 3 Å resolution, consists of a novel combination of two Ig-like domains, one characteristic of adhesion molecules and the other previously seen only in antigen receptors. In the crystal lattice, sB7-l unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. The structural data suggest a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4 homodimers, along with the relatively high affinity of these interactions, favours the formation of very stable inhibitory signaling complexes.
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References
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© 2001 Springer Japan
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Ikemizu, S., Yvonne Jones, E., Stuart, D.I., Davis, S.J. (2001). Structural studies on the leukocyte co-stimulatory molecule, B7-1. In: Cooper, M.D., Takai, T., Ravetch, J.V. (eds) Activating and Inhibitory Immunoglobulin-like Receptors. Springer, Tokyo. https://doi.org/10.1007/978-4-431-53940-7_8
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DOI: https://doi.org/10.1007/978-4-431-53940-7_8
Publisher Name: Springer, Tokyo
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