The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Structure of human lactoferrin at 3.2-A resolution.
Open accessAbstract
The three-dimensional structure of human milk lactoferrin, a member of the transferrin family, has been determined crystallographically at 3.2-A resolution. The molecule has two-fold internal homology. The N- and C-terminal halves form two separate globular lobes, connected by a short alpha-helix, and carry one iron-binding site each. Each lobe has the same folding, based on two domains of similar supersecondary structure, with the iron site at the domain interface. Each iron atom is coordinated by four protein ligands: two tyrosines, one histidine, and one aspartate. A probable CO3(2-) (or HCO3-) ion is suggested by the electron density, bound to iron and adjacent to an arginine side chain and a helix N terminus. The protein folding and location of the binding sites show marked similarities with those of other binding proteins, notably the sulfate-binding protein from Salmonella typhimurium.
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Cites
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Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins
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Préparation et propriétés de la lactosidérophiline (lactotransferrine) du lait de femme
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Cited by
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804
Lactoferrin a multiple bioactive protein: an overview
García-Montoya, I. A., Cendón, T. S., Arévalo-Gallegos, S., & Rascón-Cruz, Q. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.06.018 · Cited by 473
Lactoferrin: Multifunctional roles of lactoferrin: a critical overview
Ward, P. P., Paz, E., & Conneely, O. M. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5369-8 · Cited by 443
Transferrin/transferrin receptor‐mediated drug delivery
Li, H., & Qian, Z. M. (2002) · Medicinal Research Reviews · doi:10.1002/med.10008 · Cited by 441
Lactoferrin: Lactoferrin: a modulator of immune and inflammatory responses
Legrand, D., Elass, E., Carpentier, M., & Mazurier, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5370-2 · Cited by 420
Metadata
- Authors
- Anderson, B. F., Baker, H. M., Dodson, E. J., Norris, G. E., Rumball, S. V., Waters, J. M., & Baker, E. N.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1987-04
- Volume
- 84
- Issue
- 7
- Pages
- 1769-1773
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2033546588
- Cited by
- 386
- References
- 12
- FWCI
- 24.61
- Type
- journal article
- Language
- en
- Open access
- green
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- Anderson, B. F., Baker, H. M., Dodson, E. J., Norris, G. E., Rumball, S. V., Waters, J. M., & Baker, E. N. (1987). Structure of human lactoferrin at 3.2-A resolution. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.84.7.1769
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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