8brc: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8brc]] 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=8BRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRC FirstGlance]. <br> | <table><tr><td colspan='2'>[[8brc]] 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=8BRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BRC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NH3:AMMONIA'>NH3</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.17Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NH3:AMMONIA'>NH3</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</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=8brc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8brc OCA], [https://pdbe.org/8brc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8brc RCSB], [https://www.ebi.ac.uk/pdbsum/8brc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8brc ProSAT]</span></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=8brc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8brc OCA], [https://pdbe.org/8brc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8brc RCSB], [https://www.ebi.ac.uk/pdbsum/8brc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8brc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 8brc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8brc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transferrin 3D structures|Transferrin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 17:24, 6 November 2024
Crystal structure of the adduct between human serum transferrin and cisplatinCrystal structure of the adduct between human serum transferrin and cisplatin
Structural highlights
DiseaseTRFE_HUMAN Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:209300. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.[1] [2] FunctionTRFE_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. Publication Abstract from PubMedThe molecular mechanism of how human serum transferrin (hTF) recognizes cisplatin at the atomic level is still unclear. Here, we report the molecular structure of the adduct formed upon the reaction of hTF with cisplatin. Pt binds the side chain of Met256 (at the N-lobe), without altering the protein overall conformation. Cisplatin Binding to Human Serum Transferrin: A Crystallographic Study.,Troisi R, Galardo F, Ferraro G, Sica F, Merlino A Inorg Chem. 2023 Jan 16;62(2):675-678. doi: 10.1021/acs.inorgchem.2c04206. Epub , 2023 Jan 5. PMID:36602395[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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