Mutational analysis of the fractalkine chemokine domain. Basic amino acid residues differentially contribute to CX3CR1 binding, signaling, and cell adhesion.

@article{Harrison2001MutationalAO,
  title={Mutational analysis of the fractalkine chemokine domain. Basic amino acid residues differentially contribute to CX3CR1 binding, signaling, and cell adhesion.},
  author={Jeffrey K. Harrison and Alan M. Fong and Philip A. Swain and Shujuan Chen and Yangyang R Yu and Mina N Salafranca and William B. Greenleaf and Toshio Imai and Dhavalkumar D. Patel},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 24},
  pages={21632-41}
}
Fractalkine (FKN/CX3CL1) is a unique member of the chemokine gene family and contains a chemokine domain (CD), a mucin-like stalk, a single transmembrane region, and a short intracellular C terminus. This structural distinction affords FKN the property of mediating capture and firm adhesion of FKN receptor (CX3CR1)-expressing cells under physiological flow conditions. Shed forms of FKN also exist, and these promote chemotaxis of CX3CR1-expressing leukocytes. The goal of the present study was to… CONTINUE READING