2hav

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(New page: 200px<br /> <applet load="2hav" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hav, resolution 2.7&Aring;" /> '''Apo-Human Serum Tran...)
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<applet load="2hav" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Apo-Human Serum Transferrin (Glycosylated)'''<br />
'''Apo-Human Serum Transferrin (Glycosylated)'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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2HAV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CIT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HAV OCA].
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2HAV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAV OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Everse, S.J.]]
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[[Category: Everse, S J.]]
[[Category: Wally, J.]]
[[Category: Wally, J.]]
[[Category: CIT]]
[[Category: CIT]]
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[[Category: serotransferrin]]
[[Category: serotransferrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:29:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:39:58 2008''

Revision as of 15:39, 21 February 2008

Image:2hav.gif

2hav, resolution 2.7Å

Drag the structure with the mouse to rotate

Apo-Human Serum Transferrin (Glycosylated)

Contents

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 and 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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