Three-dimensional structures lactoferrin

Spik, G., Coddeville, B., Mazurier, J., Bourne, Y., Cambillaut, C., and Montreuil, J. 1994a. Primary and three-dimensional structure of lactotransferrin (lactoferrin) glycans. Adv. Exp. Med. Biol. 357, 21-32. 

The most detailed description of a complete transferrin molecule is that of human lactoferrin, at 2.8-A resolution (78), and most of the data in the following sections come from this work and from refinement of the same structure at 2.1-A resolution (79). As would be expected from the high level of sequence similarity, the three-dimensional structure of rabbit serum transferrin (68), although at lower resolution (3.3 A), is completely consistent with that of lactoferrin the differences are at the level of individual amino acid changes, together with some differences in lobe and domain orientations. These are discussed below (Section III.B.l). 

Three-dimensional structure of lactotransferrin. Top schematic representation of the folding pattern of each lactoferrin lobe Domain I is based on a beta-sheet of four parallel and two antiparallel domains Domain II is formdd from four parallel and one antiparallel strand. Bottom stereo Ca diagram of the N lobe of lactoferrin ( ) iron atom between domain I (residues 6-90-I-) and domain II (residues 91-251) ( ) disulfide bridges ( ) carbohydrate attachment site. See Reference 39. 

Moore SA, Anderson BF, Groom CR et al (1997) Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolutirat. J Mol Biol 274(2) 222-236... 

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