1d4n
From Proteopedia
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|PDB= 1d4n |SIZE=350|CAPTION= <scene name='initialview01'>1d4n</scene>, resolution 2.00Å | |PDB= 1d4n |SIZE=350|CAPTION= <scene name='initialview01'>1d4n</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene> | + | |LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1a8e|1A8E]], [[1a8f|1A8F]], [[1d3k|1D3K]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4n OCA], [http://www.ebi.ac.uk/pdbsum/1d4n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d4n RCSB]</span> | ||
}} | }} | ||
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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== | ||
| - | Known diseases associated with this structure: Atransferrinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190000 190000]], Iron deficiency anemia, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190000 190000]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Woodworth, R C.]] | [[Category: Woodworth, R C.]] | ||
[[Category: Yang, H W.]] | [[Category: Yang, H W.]] | ||
| - | [[Category: CO3]] | ||
| - | [[Category: FE]] | ||
[[Category: carbonate]] | [[Category: carbonate]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: transferrin]] | [[Category: transferrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:34:37 2008'' |
Revision as of 16:34, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1A8E, 1A8F, 1D3K
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN SERUM TRANSFERRIN
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.
About this Structure
1D4N is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Sun Mar 30 19:34:37 2008
