2bjj
From Proteopedia
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- | [[Image:2bjj.gif|left|200px]] | + | [[Image:2bjj.gif|left|200px]] |
- | + | ||
- | '''STRUCTURE OF RECOMBINANT HUMAN LACTOFERRIN PRODUCED IN THE MILK OF TRANSGENIC COWS''' | + | {{Structure |
+ | |PDB= 2bjj |SIZE=350|CAPTION= <scene name='initialview01'>2bjj</scene>, resolution 2.40Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+X'>AC1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=CO3:CARBONATE ION'>CO3</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF RECOMBINANT HUMAN LACTOFERRIN PRODUCED IN THE MILK OF TRANSGENIC COWS''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2BJJ is a [ | + | 2BJJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJJ OCA]. |
==Reference== | ==Reference== | ||
- | The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin., Thomassen EA, van Veen HA, van Berkel PH, Nuijens JH, Abrahams JP, Transgenic Res. 2005 Aug;14(4):397-405. PMID:[http:// | + | The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin., Thomassen EA, van Veen HA, van Berkel PH, Nuijens JH, Abrahams JP, Transgenic Res. 2005 Aug;14(4):397-405. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16201406 16201406] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metal-binding protein]] | [[Category: metal-binding protein]] | ||
[[Category: polymorphism]] | [[Category: polymorphism]] | ||
- | [[Category: transgenic | + | [[Category: transgenic cow]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:52 2008'' |
Revision as of 14:02, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF RECOMBINANT HUMAN LACTOFERRIN PRODUCED IN THE MILK OF TRANSGENIC COWS
Contents |
Overview
Human lactoferrin (hLF) is an iron-binding glycoprotein involved in the host defence against infection and excessive inflammation. As the availability of (human milk-derived) natural hLF is limited, alternative means of production of this biopharmaceutical are extensively researched. Here we report the crystal structure of recombinant hLF (rhLF) expressed in the milk of transgenic cows at a resolution of 2.4 A. To our knowledge, the first reported structure of a recombinant protein produced in milk of transgenic livestock. Even though rhLF contains oligomannose- and hybrid-type N-linked glycans next to complex-type glycans, which are the only glycans found on natural hLF, the structures are identical within the experimental error (r.m.s. deviation of only 0.28 A for the main-chain atoms). Of the differences in polymorphic amino acids between the natural and rhLF variant used, only the side-chain of Asp561 could be modeled into the rhLF electron density map. Taken together, the results confirm the structural integrity of the rhLF variant used in this study. It also confirms the validity of the transgenic cow mammary gland as a vehicle to produce recombinant human proteins.
Disease
Known disease associated with this structure: Deafness, autosomal dominant 1 OMIM:[602121]
About this Structure
2BJJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin., Thomassen EA, van Veen HA, van Berkel PH, Nuijens JH, Abrahams JP, Transgenic Res. 2005 Aug;14(4):397-405. PMID:16201406
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