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| | {{STRUCTURE_1fqe| PDB=1fqe | SCENE= }} | | {{STRUCTURE_1fqe| PDB=1fqe | SCENE= }} |
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| - | '''CRYSTAL STRUCTURES OF MUTANT (K206A) THAT ABOLISH THE DILYSINE INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN'''
| + | ===CRYSTAL STRUCTURES OF MUTANT (K206A) THAT ABOLISH THE DILYSINE INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN=== |
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| - | ==Overview==
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| - | Human transferrin (Tf) is responsible for the binding and transport of iron in the bloodstream of vertebrates. Delivery of this bound iron to cells occurs by a process of receptor-mediated endocytosis during which Tf releases its iron at the reduced endosomal pH of approximately 5.6. Iron release from Tf involves a large conformational change in which the two domains that enclose the binding site in each lobe move apart. We have examined the role of two lysines, Lys206 and Lys296, that form a hydrogen-bonded pair close to the N-lobe binding site of human Tf and have been proposed to form a pH-sensitive trigger for iron release. We report high-resolution crystal structures for the K206A and K296A mutants of the N-lobe half-molecule of Tf, hTf/2N, and quantitative iron release data on these mutants and the double mutant K206A/K296A. The refined crystal structures (for K206A, R = 19.6% and R(free) = 23.7%; for K296A, R= 21.2% and R(free) = 29.5%) reveal a highly conserved hydrogen bonding network in the dilysine pair region that appears to be maintained even when individual hydrogen bonding groups change. The iron release data show that the mutants retain iron to a pH 1 unit lower than the pH limit of wild type hTf/2N, and release iron much more slowly as a result of the loss of the dilysine interaction. Added chloride ions are shown to accelerate iron release close to the pH at which iron is naturally lost and the closed structure becomes destabilized, and to retard it at higher pH.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11327820}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11327820 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11327820}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: N-lobe]] | | [[Category: N-lobe]] |
| | [[Category: Transferrin]] | | [[Category: Transferrin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:38:36 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:46:55 2008'' |
Revision as of 00:46, 1 July 2008
Template:STRUCTURE 1fqe
CRYSTAL STRUCTURES OF MUTANT (K206A) THAT ABOLISH THE DILYSINE INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN
Template:ABSTRACT PUBMED 11327820
About this Structure
1FQE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrin., Nurizzo D, Baker HM, He QY, MacGillivray RT, Mason AB, Woodworth RC, Baker EN, Biochemistry. 2001 Feb 13;40(6):1616-23. PMID:11327820
Page seeded by OCA on Tue Jul 1 03:46:55 2008
