X-ray solution scattering reveals conformational changes upon iron uptake in lactoferrin, serum and ovo-transferrins
Abstract
X-ray solution scattering has been used for studying the structural changes that take place upon uptake and release of iron from serum and chicken ovo-transferrin and human lactoferrin. In the case of chicken ovo-transferrin, data have been obtained for both the intact protein and the isolated N and C-lobes with and without iron. These studies reveal that both lobes undergo a change that is consistent with an opening of the inter-domain cleft when iron is removed from the protein. We suggest that the conformational change of the protein increases the specificity of receptor binding and that the closed configuration of the iron-loaded protein is one, or perhaps the, decisive step in the mechanism for receptor-mediated endocytosis.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Cp functions as an antioxidant because it converts Fe2+ to Fe3+, thereby decreasing the potential formation of reactive oxygen species via Fenton chemistry.
“Cp also functions as an antioxidant, because it converts Fe2+ to Fe3+, thereby decreasing the potential formation of reactive oxygen species (ROS) via Fenton chemistry (118).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [118]
The citation lists haven’t been fetched yet
References 25 · Cited by 139
- Authors
- Grossmann, J. G., Neu, M., Pantos, E., Schwab, F. J., Evans, R. W., Townes-Andrews, E., Lindley, P. F., Appel, H., Thies, W.-G., & Hasnain, S. S.
- Affiliations
- Daresbury Laboratory (GB)
- Karlsruhe Institute of Technology (DE)
- Guy's Hospital (GB)
- Birkbeck, University of London (GB)
- Corresponding author
- Hasnain, S.Samar
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1992-06
- Volume
- 225
- Issue
- 3
- Pages
- 811-819
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2060166905
- Cited by
- 139
- References
- 25
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 3 · 2020: 2 · 2019: 4 · 2017: 3 · 2016: 4 · 2014: 3 · 2013: 1 · 2012: 3
- FWCI
- 3.73
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- University of Huddersfield Repository (University of Huddersfield) (submittedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- lactoferrin, transferrin, iron binding, conformational change, N-lobe, C-lobe, receptor-mediated endocytosis, iron absorption, protein structure
- MeSH terms
- Animals, Apoproteins, Chickens, Computer Simulation, Humans, Iron, Lactoferrin, Models, Molecular, Motion, Peptide Fragments, Protein Conformation, Scattering, Radiation, Solutions, Transferrin, X-Rays, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
