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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-5-5
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pubmed:abstractText |
The X-ray crystallographic structures of two mutants (K206Q and H207E) of the N-lobe of human transferrin (hTF/2N) have been determined to high resolution (1.8 and 2.0 A, respectively). Both mutant proteins bind iron with greater affinity than native hTF/2N. The structures of the K206Q and H207E mutants show interactions (both H-bonding and electrostatic) that stabilize the interaction of Lys296 in the closed conformation, thereby stabilizing the iron bound forms.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-10029548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-10423249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-1404372,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-1932003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-2334724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-3179277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-7578047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-7762421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-8218271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-8343132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-8535154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-8812842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9154935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9283096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9398207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9444770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9461487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9609685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9642266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9753457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9760232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10739246-9760252
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
49-52
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
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pubmed:year |
2000
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pubmed:articleTitle |
Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron.
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pubmed:affiliation |
Department of Biochemistry & Molecular Biology, University of British Columbia, Vancouver, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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