Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21).

@article{Clemenza2000StructureguidedIO,
  title={Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21).},
  author={Liliana Clemenza and David E. Isenman},
  journal={Journal of immunology},
  year={2000},
  volume={165 7},
  pages={3839-48}
}
A vital role for complement in adaptive humoral immunity is now beyond dispute. The crucial interaction is that between B cell and follicular dendritic cell-resident complement receptor 2 (CR2, CD21) and its Ag-associated ligands iC3b and C3dg, where the latter have been deposited as a result of classical pathway activation. Despite the obvious importance of this interaction, the location of a CR2 binding site within C3d, a proteolytic limit fragment of C3dg retaining CR2 binding activity, has… CONTINUE READING