@misc{10481/72237,
year = {2021},
month = {12},
url = {http://hdl.handle.net/10481/72237},
abstract = {Human serum transferrin (Tf) is a bilobed glycoprotein whose function is to transport
iron through receptor-mediated endocytosis. The mechanism for iron release is pH-dependent and
involves conformational changes in the protein, thus making it an attractive system for possible
biomedical applications. In this contribution, two powerful X-ray techniques, namely Macromolecular
X-ray Crystallography (MX) and Small Angle X-ray Scattering (SAXS), were used to study the
conformational changes of iron-free (apo) and iron-loaded (holo) transferrin in crystal and solution
states, respectively, at three different pH values of physiological relevance. A crystallographic model
of glycosylated apo-Tf was obtained at 3.0 Å resolution, which did not resolve further despite many
efforts to improve crystal quality. In the solution, apo-Tf remained mostly globular in all the pH
conditions tested; however, the co-existence of closed, partially open, and open conformations was
observed for holo-Tf, which showed a more elongated and flexible shape overall.},
organization = {DGAPA-PAPIIT project No. 207922.},
publisher = {MDPI},
keywords = {Small-Angle X-ray Scattering},
keywords = {X-ray crystallography},
keywords = {Human serum transferrin},
keywords = {Conformation change},
keywords = {pH-dependence},
title = {X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin},
doi = {10.3390/ijms222413392},
author = {Campos Escamilla, Camila and González Ramírez, Luis Antonio and López Sánchez, Carmen and Gavira Gallardo, José Antonio and Moreno, Abel},
}