The B-lymphocyte activation antigen B7-1 (CD80) provides regulatory signals for T lymphocytes as a consequence of binding to the CD28 and CTLA4 ligands of T cells. After engagement of T-cell receptor with an antigen in association with MHC class II, a second signal mediated through the binding of B7-1 to CD28 greatly upregulates the production of multiple lymphokines (1). The relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity. CTLA-4 forms homodimers through a newly defined interface of highly conserved residues. This zipper-like oligomerization provides the structural basis for forming unusually stable signaling complexes at the T-cell surface, underscoring the importance of potent inhibitory signaling in human immune responses (2).
Toll-like receptor signaling pathway
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