Linked Life Data

8515439

Source:http://linkedlifedata.com/resource/pubmed/id/8515439

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pubmed-article:8515439pubmed:abstractTextRecent X-ray crystallographic and solution X-ray scattering studies have shown that transferrins (serum transferrin, lactoferrin and ovotransferrin) undergo a major conformational change when iron is incorporated into the molecule. Apo-proteins show a structure with open interdomain clefts which close when iron is bound. The closed conformation has been suggested as an important step in the receptor recognition. Here, we report X-ray solution scattering experiments of the mutated N-terminal fragment of human serum transferrin with Asp63-->Ser (Cys). The data provide the first direct experimental evidence for the existence of a trigger mechanism for the closure of the interdomain cleft and that this trigger mechanism is disrupted by mutation of Asp63, the only ligand of iron from domain I.lld:pubmed
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pubmed-article:8515439pubmed:authorpubmed-author:MasonA BABlld:pubmed
pubmed-article:8515439pubmed:authorpubmed-author:GrossmannJ...lld:pubmed
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pubmed-article:8515439pubmed:pagination554-8lld:pubmed
pubmed-article:8515439pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:8515439pubmed:articleTitleAsp ligand provides the trigger for closure of transferrin molecules. Direct evidence from X-ray scattering studies of site-specific mutants of the N-terminal half-molecule of human transferrin.lld:pubmed
pubmed-article:8515439pubmed:affiliationMolecular Biophysics Group, SERC Daresbury Laboratory, Warrington, Cheshire, U.K.lld:pubmed
pubmed-article:8515439pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8515439pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:8515439pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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