ABSTRACT
This chapter describes the chemokine structures that have been determined to date and discusses the structural differences in terms of observed functional differences between the chemokine proteins. The three-dimensional structures of several chemokines, from both the C-X-C and C-C subfamilies, determined using nuclear magnetic resonance spectroscopic or X-ray crystallographic techniques. The tertiary conformations of the monomeric subunits of each of the chemokines are similar. Investigations of C-C chemokine structure are less numerous than in the C-X-C area. Comparisons have been made within each chemokine subfamily with the aim of highlighting structural differences that may be important for specific activity. Binding of chemokines to cell surface glycosaminoglycan (GAG) is an important aspect of chemokine function, and any discussion of the functional importance of structure must address such binding events. Most C-C chemokines contain at least three basic residues in this region, suggesting that this may be a GAG binding site common to all members of this subfamily.
