Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053298 | FEBS Letters | 2005 | 4 Pages |
Abstract
The G6b gene, located in the human Major Histocompatibility Complex, encodes a receptor of the immunoglobulin (Ig) superfamily. In this study, we show using a variety of techniques that the extracellular domain of the G6b protein, containing a single Ig-like domain, binds to heparin with high affinity. In an ELISA assay, this binding was displaceable with soluble heparin with an IC50 value of approximately 0.5 μg/ml. Other sulfated glycans showed weaker or no competition. The observed interaction between G6b and heparin is strongly salt dependent suggesting a mainly electrostatic interaction. Heparin might modulate the interaction of G6b with its as yet unidentified protein ligand.
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Authors
Edwin C.J.M. de Vet, Stephen A.B. Newland, Paul A. Lyons, Begoña Aguado, R. Duncan Campbell,