9h4v
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the adduct formed upon reaction of aurothiomalate with human serum transferrin (apo-form)== | |
| - | + | <StructureSection load='9h4v' size='340' side='right'caption='[[9h4v]], [[Resolution|resolution]] 3.02Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9h4v]] is a 2 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=9H4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H4V FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.02Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9h4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h4v OCA], [https://pdbe.org/9h4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h4v RCSB], [https://www.ebi.ac.uk/pdbsum/9h4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h4v ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Disease == |
| - | [[Category: Messori | + | [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> |
| - | [[Category: | + | == Function == |
| + | [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. | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Galardo F]] | ||
| + | [[Category: Merlino A]] | ||
| + | [[Category: Messori L]] | ||
| + | [[Category: Sica F]] | ||
| + | [[Category: Troisi R]] | ||
Current revision
Crystal structure of the adduct formed upon reaction of aurothiomalate with human serum transferrin (apo-form)
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Categories: Homo sapiens | Large Structures | Galardo F | Merlino A | Messori L | Sica F | Troisi R
