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| {{STRUCTURE_1ryx| PDB=1ryx | SCENE= }} | | {{STRUCTURE_1ryx| PDB=1ryx | SCENE= }} |
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| '''Crystal structure of hen serum transferrin in apo- form'''
| | ===Crystal structure of hen serum transferrin in apo- form=== |
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| ==Overview==
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| The iron binding and release of serum transferrin are pH-dependent and accompanied by a conformational change between the iron-bound (holo-) and iron-free (apo-) forms. We have determined the crystal structure of apo-hen serum transferrin (hAST) at 3.5A resolution, which is the first reported structure to date of any full molecule of an apo-serum transferrin and studied its pH-dependent iron release by UV-vis absorption and near UV-CD spectroscopy. The crystal structure of hAST shows that both the lobes adopt an open conformation and the relative orientations of the domains are different from those of apo-human serum transferrin and human apolactoferrin but similar to that of hen apo-ovotransferrin. Spectroscopic analysis reveals that in hen serum transferrin, release of the first iron starts at a pH approximately 6.5 and continues over a broad pH range (6.5-5.2). The complete release of the iron, however, occurs at pH approximately 4.0. The near UV-CD spectra show alterations in the microenvironment of the aromatic residues surrounding the iron-binding sites. | | The line below this paragraph, {{ABSTRACT_PUBMED_15044101}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15044101 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15044101}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Domain orientation]] | | [[Category: Domain orientation]] |
| [[Category: Hen serum transferrin]] | | [[Category: Hen serum transferrin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:04:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:27:10 2008'' |