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http://purl.uniprot.org/citations/10089347http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10089347http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10089347http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.org/dc/terms/identifier"doi:10.1107/s0907444998011226"xsd:string
http://purl.uniprot.org/citations/10089347http://purl.org/dc/terms/identifier"doi:10.1107/s0907444998011226"xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Jameson G.B."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Jameson G.B."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Baker E.N."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Baker E.N."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Baker H.M."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Baker H.M."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Sun X.L."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Sun X.L."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Shewry S.C."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/author"Shewry S.C."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/pages"403-407"xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/pages"403-407"xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/title"Structure of recombinant human lactoferrin expressed in Aspergillus awamori."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/title"Structure of recombinant human lactoferrin expressed in Aspergillus awamori."xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/volume"55"xsd:string
http://purl.uniprot.org/citations/10089347http://purl.uniprot.org/core/volume"55"xsd:string