The amino-terminal immunoglobulin-like domain of activated leukocyte cell adhesion molecule binds specifically to the membrane-proximal scavenger receptor cysteine-rich domain of CD6 with a 1:1 stoichiometry.

@article{Bowen1996TheAI,
  title={The amino-terminal immunoglobulin-like domain of activated leukocyte cell adhesion molecule binds specifically to the membrane-proximal scavenger receptor cysteine-rich domain of CD6 with a 1:1 stoichiometry.},
  author={Michael A. Bowen and J{\"u}rgen Bajorath and Anthony W. Siadak and Brett Modrell and A R Malacko and Hans Marquardt and Steven G. Nadler and Alejandro Aruffo},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 29},
  pages={17390-6}
}
Activated leukocyte cell adhesion molecule (ALCAM) was recently identified as a ligand for CD6, a signaling receptor expressed on T cells, a subset of B cells, and some cells in the brain. Receptor-ligand binding assays, antibody blocking experiments, and examination of the tissue distribution of these two cell surface proteins suggest that CD6-ALCAM interactions play an important role in mediating the binding of thymocytes to thymic epithelial cells and of T cells to activated leukocytes… CONTINUE READING
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