Molecular Modeling of Human Serum Transferrin for Rationalizing the Changes in Its Physicochemical Properties Induced by Iron Binding. Implication of the Mechanism of Binding to Its Receptor
- 1 April 2000
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 19 (3) , 215-223
- https://doi.org/10.1023/a:1007059820834
Abstract
In order to rationalize the physicochemical properties of human serum-transferrin (STf) and the STf-receptor (TfR) recognition process, we have tried to predict the 3D structures of apo- and...Keywords
This publication has 17 references indexed in Scilit:
- The interpretation of protein structures: Estimation of static accessibilityPublished by Elsevier ,2004
- Alternative Structural State of TransferrinPublished by Elsevier ,1999
- Two High-Resolution Crystal Structures of the Recombinant N-Lobe of Human Transferrin Reveal a Structural Change Implicated in Iron Release,Biochemistry, 1998
- Crystal Structure of Diferric Hen Ovotransferrin at 2.4 Å ResolutionJournal of Molecular Biology, 1995
- Calorimetric Studies of Serum Transferrin and Ovotransferrin. Estimates of Domain Interactions, and Study of the Kinetic Complexities of Ferric Ion BindingBiochemistry, 1994
- Macroscopic models of aqueous solutions: biological and chemical applicationsThe Journal of Physical Chemistry, 1993
- X-ray solution scattering reveals conformational changes upon iron uptake in lactoferrin, serum and ovo-transferrinsJournal of Molecular Biology, 1992
- Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational changeActa crystallographica Section B, Structural science, crystal engineering and materials, 1991
- Apolactoferrin structure demonstrates ligand-induced conformational change in transferrinsNature, 1990
- The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesisCell, 1981