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Three-dimensional structure of lactoferrin in various functional states.

Authors
  • Baker, E N
  • Anderson, B F
  • Baker, H M
  • Day, C L
  • Haridas, M
  • Norris, G E
  • Rumball, S V
  • Smith, C A
  • Thomas, D H
Type
Published Article
Journal
Advances in experimental medicine and biology
Publication Date
Jan 01, 1994
Volume
357
Pages
1–12
Identifiers
PMID: 7762421
Source
Medline
License
Unknown

Abstract

The three-dimensional structures of various forms of lactoferrin, determined by high resolution crystallographic studies, have been compared in order to determine the relationship between structure and biological function. These comparisons include human apo and diferric lactoferrins, metal and anion substituted lactoferrins, the N-terminal half molecule of human lactoferrin, and bovine diferric lactoferrin. The structures themselves define the nature and location of the iron binding sites and allow anti-bacterial and putative receptor-binding regions to be mapped on to the molecular surface. The structural comparisons show that small internal adjustments can allow the accommodation of different metals and anions without altering the overall molecular structure, whereas large-scale conformational changes are associated with metal binding and release, and smaller, but significant, movements accompany species variations. The results also focus on differences in flexibility between the two lobes, and on the importance of interactions in the inter-lobe region in modulating iron release from the N-lobe and in possibly enabling binding at one site to be signalled to the other.

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