1b0l
From Proteopedia
(New page: 200px<br /> <applet load="1b0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0l, resolution 2.2Å" /> '''RECOMBINANT HUMAN DI...) |
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| - | [[Image:1b0l.gif|left|200px]]<br /> | + | [[Image:1b0l.gif|left|200px]]<br /><applet load="1b0l" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1b0l" size=" | + | |
caption="1b0l, resolution 2.2Å" /> | caption="1b0l, resolution 2.2Å" /> | ||
'''RECOMBINANT HUMAN DIFERRIC LACTOFERRIN'''<br /> | '''RECOMBINANT HUMAN DIFERRIC LACTOFERRIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human lactoferrin (hLf) has considerable potential as a therapeutic agent. | + | Human lactoferrin (hLf) has considerable potential as a therapeutic agent. Overexpression of hLf in the fungus Aspergillus awamori has resulted in the availability of very large quantities of this protein. Here, the three-dimensional structure of the recombinant hLf has been determined by X-ray crystallography at a resolution of 2.2 A. The final model, comprising 5339 protein atoms (residues 1-691, 294 solvent molecules, two Fe3+and two CO32- ions), gives an R factor of 0.181 (free R = 0.274) after refinement against 32231 reflections in the resolution range 10-2.2 A. Superposition of the recombinant hLf structure onto the native milk hLf structure shows a very high level of correspondence; the main-chain atoms for the entire polypeptide can be superimposed with an r.m.s. deviation of only 0.3 A and there are no significant differences in side-chain conformations or in the iron-binding sites. Dynamic properties, as measured by B-value distributions or iron-release kinetics, also agree closely. This shows that the structure of the protein is not affected by the mode of expression, the use of strain-improvement procedures or the changes in glycosylation due to the fungal system. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B0L 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 FE and CO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1B0L 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=FE:'>FE</scene> and <scene name='pdbligand=CO3:'>CO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, E | + | [[Category: Baker, E N.]] |
| - | [[Category: Jameson, G | + | [[Category: Jameson, G B.]] |
[[Category: Sun, X.]] | [[Category: Sun, X.]] | ||
[[Category: CO3]] | [[Category: CO3]] | ||
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[[Category: transferrin]] | [[Category: transferrin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:14 2008'' |
Revision as of 09:50, 21 February 2008
|
RECOMBINANT HUMAN DIFERRIC LACTOFERRIN
Contents |
Overview
Human lactoferrin (hLf) has considerable potential as a therapeutic agent. Overexpression of hLf in the fungus Aspergillus awamori has resulted in the availability of very large quantities of this protein. Here, the three-dimensional structure of the recombinant hLf has been determined by X-ray crystallography at a resolution of 2.2 A. The final model, comprising 5339 protein atoms (residues 1-691, 294 solvent molecules, two Fe3+and two CO32- ions), gives an R factor of 0.181 (free R = 0.274) after refinement against 32231 reflections in the resolution range 10-2.2 A. Superposition of the recombinant hLf structure onto the native milk hLf structure shows a very high level of correspondence; the main-chain atoms for the entire polypeptide can be superimposed with an r.m.s. deviation of only 0.3 A and there are no significant differences in side-chain conformations or in the iron-binding sites. Dynamic properties, as measured by B-value distributions or iron-release kinetics, also agree closely. This shows that the structure of the protein is not affected by the mode of expression, the use of strain-improvement procedures or the changes in glycosylation due to the fungal system.
Disease
Known disease associated with this structure: Deafness, autosomal dominant 1 OMIM:[602121]
About this Structure
1B0L is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of recombinant human lactoferrin expressed in Aspergillus awamori., Sun XL, Baker HM, Shewry SC, Jameson GB, Baker EN, Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):403-7. PMID:10089347
Page seeded by OCA on Thu Feb 21 11:50:14 2008
Categories: Homo sapiens | Single protein | Baker, E N. | Jameson, G B. | Sun, X. | CO3 | FE | Binding protein | Metalloprotein | Transferrin
