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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 (sB7-1), solved to 3 Angstrom 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, sB7-1 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.

Type

Conference paper

Publication Date

2001

Pages

63 - 72

Keywords

CELLS, crystal structure, CRYSTALLIZATION, SOLUBLE FORM, CD28, CTLA-4, B7-1, CD80, co-stimulatory molecule