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spinqualitylabelsall models 2hav, resolution 2.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Apo-Human Serum Transferrin (Glycosylated)

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Serum transferrin reversibly binds iron in each of two lobes and delivers, it to cells by a receptor-mediated, pH-dependent process. The binding and, release of iron result in a large conformational change in which two, subdomains in each lobe close or open with a rigid twisting motion around, a hinge. We report the structure of human serum transferrin (hTF) lacking, iron (apo-hTF), which was independently determined by two methods: 1) the, crystal structure of recombinant non-glycosylated apo-hTF was solved at, 2.7-A resolution using a multiple wavelength anomalous dispersion phasing, strategy, by substituting the nine methionines in hTF with, selenomethionine and 2) the structure of glycosylated apo-hTF (isolated, from serum) was determined to a resolution of 2.7A by molecular, replacement using the human apo-N-lobe and the rabbit holo-C1-subdomain as, search models. These two crystal structures are essentially identical., They represent the first published model for full-length human transferrin, and reveal that, in contrast to family members (human lactoferrin and hen, ovotransferrin), both lobes are almost equally open: 59.4 degrees and 49.5, degrees rotations are required to open the N- and C-lobes, respectively, (compared with closed pig TF). Availability of this structure is critical, to a complete understanding of the metal binding properties of each lobe, of hTF; the apo-hTF structure suggests that differences in the hinge, regions of the N- and C-lobes may influence the rates of iron binding and, release. In addition, we evaluate potential interactions between apo-hTF, and the human transferrin receptor.

Disease

Known diseases associated with this structure: Atransferrinemia OMIM:[190000], Iron deficiency anemia, susceptibility to OMIM:[190000]

About this Structure

2HAV is a Single protein structure of sequence from Homo sapiens with CIT and GOL as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding., Wally J, Halbrooks PJ, Vonrhein C, Rould MA, Everse SJ, Mason AB, Buchanan SK, J Biol Chem. 2006 Aug 25;281(34):24934-44. Epub 2006 Jun 22. PMID:16793765

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