1d3k: Difference between revisions

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==Overview==
==Overview==
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.
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.


==Disease==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brayer, G.D.]]
[[Category: Brayer, G D.]]
[[Category: Chen, J.]]
[[Category: Chen, J.]]
[[Category: Luo, Y.]]
[[Category: Luo, Y.]]
[[Category: MacGillivray, R.T.A.]]
[[Category: MacGillivray, R T.A.]]
[[Category: Mason, A.]]
[[Category: Mason, A.]]
[[Category: Murphy, M.E.P.]]
[[Category: Murphy, M E.P.]]
[[Category: Wang, Y.]]
[[Category: Wang, Y.]]
[[Category: Woodworth, R.C.]]
[[Category: Woodworth, R C.]]
[[Category: Yang, H.W.]]
[[Category: Yang, H W.]]
[[Category: CO3]]
[[Category: CO3]]
[[Category: FE]]
[[Category: FE]]
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[[Category: transferrin]]
[[Category: transferrin]]


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Revision as of 13:12, 21 February 2008

File:1d3k.jpg


1d3k, resolution 1.8Å

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HUMAN SERUM TRANSFERRIN

OverviewOverview

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.

DiseaseDisease

Known diseases associated with this structure: Atransferrinemia OMIM:[190000], Iron deficiency anemia, susceptibility to OMIM:[190000]

About this StructureAbout this Structure

1D3K is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron., Yang AH, MacGillivray RT, Chen J, Luo Y, Wang Y, Brayer GD, Mason AB, Woodworth RC, Murphy ME, Protein Sci. 2000 Jan;9(1):49-52. PMID:10739246

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