Molecular structure, binding properties and dynamics of lactoferrin.

摘要: Lactoferrin (Lf), a prominent protein in milk, many other secretory fluids and white blood cells, is monomeric, 80-kDa glycoprotein, with single polypeptide chain of about 690 amino acid residues. Amino sequence relationships place it the wider transferrin family. Crystallographic analyses human Lf, Lfs from cow, horse, buffalo camel, reveal highly conserved three-dimensional structure, but differences detail between species. The molecule folded into homologous N- C-terminal lobes, each comprising two domains that enclose iron binding site. Iron release accompanied by domain movements close or open sites, influenced cooperative interactions lobes. Patches high positive charge on surface contribute to properties, attached glycan chains appear have little impact structure function.