A structural framework for understanding the multifunctional character of lactoferrin

摘要: Lactoferrin (Lf) is widely distributed, in mammalian milks, other secretory fluids and white blood cells, its biology complex. The three-dimensional structure of this important protein was determined 1987, giving the first atomic view any member transferrin family. This review examines how structural knowledge has contributed to our understanding Lf function, what we have yet understand. internal highly conserved, dedicated binding iron, which sequestered two almost identical sites, one each lobe molecule. processes iron release, accompanying conformational changes, are well understood. Some functional properties derive from property, both through scavenging, because dynamics altered by status. On hand, external (its molecular surface) much more variable between different Lfs, making it difficult identify functionally sites. One key feature clear - cationic N-terminus associated lactoferricin domain on N-lobe Lf. Recent work shows that region, addition role antibacterial activity probable DNA binding, also involved complex formation with proteins. Other parts surface may result differences Lfs species. Finally, be time re-examine importance glycosylation, given growing evidence many pathogens depend glycans for pathogenesis.