ABSTRACT
Significant insight into the structure and function of cell surface receptors for proinflammatory chemokines has been deduced from molecular genetic and cell biology approaches. Besides its role as a binding protein for proinflammatory chemokines, the erythrocyte chemokine receptor was demonstrated to have another identity. Despite the disagreement between the molecular modeling strategies, Duffy antigen/receptor for chemokines (DARC) has significant similarity to receptors for other chemokines and chemoattractants which signal through G-proteins and conform to molecular models predicting seven hydrophobic helices. The localization of DARC to endothelial cells that line postcapillary venules is interesting since these structures are a dynamic interface that comprise the site for leukocyte transmigration from the vascular space into the tissue space during inflammation. DARC has very little primary amino acid sequence homology with the cloned chemokine receptors: at the level of nucleotide sequence it is most closely related to the interleukin-8 receptor pseudogene, with which it shares around 28% homology.
