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http://purl.uniprot.org/citations/10089508http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10089508http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10089508http://www.w3.org/2000/01/rdf-schema#comment"The three-dimensional structure of a form of human apolactoferrin, in which one lobe (the N-lobe) has an open conformation and the other lobe (the C-lobe) is closed, has been refined at 2.0 A resolution. The refinement, by restrained least-squares methods, used synchrotron radiation X-ray diffraction data combined with a lower resolution diffractometer data set. The final refined model (5346 protein atoms from residues 1-691, two Cl-ions and 363 water molecules) gives a crystallographic R factor of 0.201 (Rfree = 0. 286) for all 51305 reflections in the resolution range 10.0-2.0 A. The conformational change in the N-lobe, which opens up the binding cleft, involves a 54 degrees rotation of the N2 domain relative to the N1 domain. This also results in a small reorientation of the two lobes relative to one another with a further approximately 730 A2 of surface area being buried as the N2 domain contacts the C-lobe and the inter-lobe helix. These new contacts also involve the C-terminal helix and provide a mechanism through which the conformational and iron-binding status of the N-lobe can be signalled to the C-lobe. Surface-area calculations indicate a fine balance between open and closed forms of lactoferrin, which both have essentially the same solvent-accessible surface. Chloride ions are bound in the anion-binding sites of both lobes, emphasizing the functional significance of these sites. The closed configuration of the C-lobe, attributed in part to weak stabilization by crystal packing interactions, has important implications for lactoferrin dynamics. It shows that a stable closed structure, essentially identical to that of the iron-bound form, can be formed in the absence of iron binding."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.org/dc/terms/identifier"doi:10.1107/s0907444998004417"xsd:string
http://purl.uniprot.org/citations/10089508http://purl.org/dc/terms/identifier"doi:10.1107/s0907444998004417"xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Jameson G.B."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Jameson G.B."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Baker E.N."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Baker E.N."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Anderson B.F."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Anderson B.F."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Norris G.E."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Norris G.E."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Thomas D.H."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/author"Thomas D.H."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/pages"1319-1335"xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/pages"1319-1335"xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/title"Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/title"Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change."xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/volume"54"xsd:string
http://purl.uniprot.org/citations/10089508http://purl.uniprot.org/core/volume"54"xsd:string
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