Lactoferrin conformational change

Figure 5.8 A schematic representation of the N-lobe polypeptide chain fold, showing the conformational change between open and closed forms of human lactoferrin. Reprinted with permission from Nature (Anderson et ah, 1990). Copyright (1990) Macmillan Magazines Limited.

Fig. 11. Schematic diagrams of the open (left) and closed (right) forms, shown for the N-lobe of human lactoferrin. In the conformational change, helix 5 in domain N2 appears to pivot on helix 11. The hinge in the two backbone strands (at Thr 90 and Pro 251) is indicated with an arrow. Taken from Anderson et al. (80).

Solution scattering measurements on half-molecules show that they undergo very similar conformational changes, on iron binding or release, to those of the corresponding lobes of intact transferrins (104). This, together with the structural correspondence noted above, makes them valid as models of single-sited transferrins. The lactoferrin half-... 

Figure 3.3. Flexibility aud Fuuctiou. Upon binding iron, the protein lactoferrin undergoes conformational changes that...

Figure 2.3 Flexibility and function. On binding iron, the protein lactoferrin undergoes a substantial change in conformation that allows other molecules to distinguish between the iron free and the iron-bound forms. [Drawn from ILFM.pdp and ILFG.pdb.]...

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