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169±1, and 190±1. The false positive boundary at 44/45 seen in this figure is introduced<br />

when a 5 th chain segment is requested.<br />

Human lactoferrin<br />

Morph ID: f964647-15593 PDB ID: 1LFG<br />

HAG hinges: 90,91,250,251<br />

Human lactoferrin (hLF) is an iron-binding glycoprotein found in exocrine fluids<br />

produced by mammals, including milk, saliva, tears, bile, pancreatic fluid, and mucous<br />

secretions. It has broad spectrum antibacterial properties and seems to regulate the<br />

absorption and excretion of iron in infants.<br />

The hinge bending motion of lactoferrin has been studied in detail. The protein consists<br />

of N- and C- terminal lobes which are highly homologous and are presumed to have<br />

arisen from gene duplication. Each lobe is further subdivided into two domains, N1 and<br />

N2, and C1 and C2. In the iron-free form, a deep cleft appears between N1 and N2. No<br />

such cleft appears in the C-lobe either in the iron free or iron bound form, but this is<br />

believed to be an artifact of crystallization. In the iron-bound form, N1 and N2 are close<br />

together about a common hinge, located between residues 90 and 91, and 250 and 251<br />

according to Gerstein et al. This is in perfect agreement with the independent annotation<br />

made in this work.<br />

186

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