Crystallographic Studies on Metal and Anion Substituted Human Lactoferrin

Abstract

The metal and anion binding function of the transferrins has been well characterised by a host of spectroscopic methods, and the members of this family of proteins are known to bind a wide variety of metal ions including the first, second and third row transition metals, the group 13 metals, the lanthanides and some of the actinides (Aisen and Harris, 1989). Crystallographic studies, on the other hand, have concentrated primarily on diferric and apolactoferrin (Anderson et al, 1989; 1990) and diferric rabbit transferrin (Bailey et al, 1988; Sarra et al, 1990). These crystallographic studies have defined the polypeptide chain folding and the metal (iron) and anion (carbonate) sites (Baker et al., this volume).