5wtd
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of human serum transferrin bound ruthenium at N-lobe== | |
| - | + | <StructureSection load='5wtd' size='340' side='right' caption='[[5wtd]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5wtd]] is a 1 chain structure with 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=5WTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WTD FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wtd OCA], [http://pdbe.org/5wtd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wtd RCSB], [http://www.ebi.ac.uk/pdbsum/5wtd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wtd ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://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 == | ||
| + | [[http://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: Hao, Q]] | ||
| + | [[Category: Lai, T P]] | ||
| + | [[Category: Sun, H]] | ||
| + | [[Category: Wang, M]] | ||
| + | [[Category: Zhang, H]] | ||
| + | [[Category: Metal transport]] | ||
| + | [[Category: Ruthenium transferrin n-lobe]] | ||
Revision as of 06:19, 20 December 2017
Structure of human serum transferrin bound ruthenium at N-lobe
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