1n7x

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{{Seed}}
 
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[[Image:1n7x.png|left|200px]]
 
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==HUMAN SERUM TRANSFERRIN, N-LOBE Y45E MUTANT==
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The line below this paragraph, containing "STRUCTURE_1n7x", creates the "Structure Box" on the page.
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<StructureSection load='1n7x' size='340' side='right'caption='[[1n7x]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1n7x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N7X FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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{{STRUCTURE_1n7x| PDB=1n7x | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n7x OCA], [https://pdbe.org/1n7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n7x RCSB], [https://www.ebi.ac.uk/pdbsum/1n7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n7x ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[https://omim.org/entry/209300 209300]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n7/1n7x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n7x ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human serum transferrin (hTF) is a bilobal iron-binding and transport protein that carries iron in the blood stream for delivery to cells by a pH-dependent mechanism. Two iron atoms are held tightly in two deep clefts by coordination to four amino acid residues in each cleft (two tyrosines, a histidine, and an aspartic acid) and two oxygen atoms from the "synergistic" carbonate anion. Other residues in the binding pocket, not directly coordinated to iron, also play critical roles in iron uptake and release through hydrogen bonding to the liganding residues. The original crystal structures of the iron-loaded N-lobe of hTF (pH 5.75 and 6.2) revealed that the synergistic carbonate is stabilized by interaction with Arg-124 and that both the arginine and the carbonate adopt two conformations (MacGillivray, R. T. A., Moore, S. A., Chen, J., Anderson, B. F., Baker, H., Luo, Y. G., Bewley, M., Smith, C. A., Murphy, M. E., Wang, Y., Mason, A. B., Woodworth, R. C., Brayer, G. D., and Baker, E. N. (1998) Biochemistry 37, 7919-7928). In the present study, we show that the two conformations are also found for a structure at pH 7.7, indicating that this finding was not strictly a function of pH. We also provide structures for two single point mutants (Y45E and L66W) designed to force Arg-124 to adopt each of the previously observed conformations. The structures of each mutant show that this goal was accomplished, and functional studies confirm the hypothesis that access to the synergistic anion dictates the rate of iron release. These studies highlight the importance of the arginine/carbonate movement in the mechanism of iron release in the N-lobe of hTF. Access to the carbonate via a water channel allows entry of protons and anions, enabling the attack on the iron.
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===HUMAN SERUM TRANSFERRIN, N-LOBE Y45E MUTANT===
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The position of arginine 124 controls the rate of iron release from the N-lobe of human serum transferrin. A structural study.,Adams TE, Mason AB, He QY, Halbrooks PJ, Briggs SK, Smith VC, MacGillivray RT, Everse SJ J Biol Chem. 2003 Feb 21;278(8):6027-33. Epub 2002 Nov 27. PMID:12458193<ref>PMID:12458193</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1n7x" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12458193}}, adds the Publication Abstract to the page
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*[[Transferrin 3D structures|Transferrin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12458193 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12458193}}
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__TOC__
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</StructureSection>
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==Disease==
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Known disease 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]]
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==About this Structure==
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1N7X is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7X OCA].
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==Reference==
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<ref group="xtra">PMID:12458193</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Adams, T E.]]
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[[Category: Large Structures]]
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[[Category: Briggs, S K.]]
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[[Category: Adams TE]]
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[[Category: Everse, S J.]]
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[[Category: Briggs SK]]
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[[Category: Halbrooks, P J.]]
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[[Category: Everse SJ]]
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[[Category: He, Q Y.]]
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[[Category: Halbrooks PJ]]
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[[Category: Macgillivray, R T.]]
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[[Category: He QY]]
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[[Category: Mason, A B.]]
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[[Category: Macgillivray RT]]
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[[Category: Smith, V C.]]
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[[Category: Mason AB]]
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[[Category: Iron transport]]
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[[Category: Smith VC]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:57:10 2009''
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Current revision

HUMAN SERUM TRANSFERRIN, N-LOBE Y45E MUTANT

PDB ID 1n7x

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