1b0l: Difference between revisions
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|PDB= 1b0l |SIZE=350|CAPTION= <scene name='initialview01'>1b0l</scene>, resolution 2.2Å | |PDB= 1b0l |SIZE=350|CAPTION= <scene name='initialview01'>1b0l</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0l OCA], [http://www.ebi.ac.uk/pdbsum/1b0l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0l RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Jameson, G B.]] | [[Category: Jameson, G B.]] | ||
[[Category: Sun, X.]] | [[Category: Sun, X.]] | ||
[[Category: binding protein]] | [[Category: binding protein]] | ||
[[Category: metalloprotein]] | [[Category: metalloprotein]] | ||
[[Category: transferrin]] | [[Category: transferrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:13 2008'' | ||
