Summary Chapter

Abstract

A goal expressed in this session was to increase attempts by all researchers in this field to correlate known structural features of the lactoferrin molecule with the mechanism(s) of physiological functions, e.g., the interaction with cells and membrane structures. Factors to consider regarding the three-dimensional structure would include the degree of domain movement (lobe flexibility) within both the N-lobe and the C-lobe, and the role of bound metal ions as structural determinants of these dynamics. The structural dynamics of the lactoferrin molecule in solution (i.e., possible mobility of loops and other domain structures) are more difficult to address and remain to be verified. While some individual amino acid residues can be very mobile, secondary structural domains appear to be relatively stable. The three-dimensional structure of the glycan moieties (different in number and sequence for bovine and human milk lactoferrins) and the effects of these posttranslational modifications on lactoferrin structure and function remain to be explored. Future priorities in the structural analysis of lactoferrin is co-crystallization of the lactoferrin-receptor complex and its structural analysis.