Abstract
Met-RANTES is a modified version of the chemokine RANTES, which has an additional amino acid at the amino terminus. To compare Met-RANTES with the native protein as well as with another antagonist, AOP RANTES, we have solved the structure of Met-RANTES at 1.6 A by X-ray crystallography and investigated the dimerization of all three proteins by fluorescence anisotropy. The dimerization of AOP-RANTES shows an altered aggregation profile. The delineation of slight differences in binding sulfate anions by Met- and AOP RANTES might be linked to specific yet different interactions between these proteins and glycosaminoglycans.