View source for 28ms


==X-ray structure of the adduct between human serum transferrin with Fe3+ bound at the C-lobe and dirhodium tetraacetate==
<StructureSection load='28ms' size='340' side='right'caption='[[28ms]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[28ms]] 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=28MS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=28MS 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]] 2.37&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=28ms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=28ms OCA], [https://pdbe.org/28ms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=28ms RCSB], [https://www.ebi.ac.uk/pdbsum/28ms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=28ms ProSAT]</span></td></tr>
</table>
== Disease ==
[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> 
== 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ru and Rh binding sites in the structure of human serum transferrin with Fe(3+) bound at the C-lobe were identified by X-ray crystallography. Several His side chains and one Met are involved in the recognition of the metal ions by the protein.

Ru and Rh binding sites in the structure of human serum transferrin with Fe(3+) bound at the C-lobe.,Banneville AS, Ferraro G, D'Elia R, Cornaciu-Hoffmann I, Pica A, Merlino A Dalton Trans. 2026 Mar 10;55(10):4051-4056. doi: 10.1039/d6dt00205f. PMID:41738634<ref>PMID:41738634</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 28ms" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ferraro G]]
[[Category: Merlino A]]