1d4n

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==Overview==
==Overview==
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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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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]]
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[[Category: Brayer, G.D.]]
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[[Category: Brayer, G D.]]
[[Category: Chen, J.]]
[[Category: Chen, J.]]
[[Category: Luo, Y.]]
[[Category: Luo, Y.]]
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[[Category: MacGillivray, R.T.A.]]
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[[Category: MacGillivray, R T.A.]]
[[Category: Mason, A.]]
[[Category: Mason, A.]]
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[[Category: Murphy, M.E.P.]]
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[[Category: Murphy, M E.P.]]
[[Category: Wang, Y.]]
[[Category: Wang, Y.]]
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[[Category: Woodworth, R.C.]]
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[[Category: Woodworth, R C.]]
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[[Category: Yang, H.W.]]
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[[Category: Yang, H W.]]
[[Category: CO3]]
[[Category: CO3]]
[[Category: FE]]
[[Category: FE]]
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[[Category: transferrin]]
[[Category: transferrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:38:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:56 2008''

Revision as of 10:13, 21 February 2008


1d4n, resolution 2.00Å

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HUMAN SERUM TRANSFERRIN

Contents

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.

Disease

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

About this Structure

1D4N is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

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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