1dr9
From Proteopedia
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CRYSTAL STRUCTURE OF A SOLUBLE FORM OF B7-1 (CD80)
Overview
B7-1 (CD80) and B7-2 (CD86) are glycoproteins expressed on, antigen-presenting cells. The binding of these molecules to the T cell, homodimers CD28 and CTLA-4 (CD152) generates costimulatory and inhibitory, signals in T cells, respectively. The crystal structure of the, extracellular region of B7-1 (sB7-1), solved to 3 A 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. Analytical ultracentrifugation, reveals that sB7-1 also dimerizes in solution. 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, favors the formation of very stable inhibitory signaling complexes.
About this Structure
1DR9 is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Structure and dimerization of a soluble form of B7-1., Ikemizu S, Gilbert RJ, Fennelly JA, Collins AV, Harlos K, Jones EY, Stuart DI, Davis SJ, Immunity. 2000 Jan;12(1):51-60. PMID:10661405
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