4x1d: Difference between revisions

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 ==Ytterbium-bound human serum transferrin==
-<StructureSection load='4x1d' size='340' side='right' caption='[[4x1d]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='4x1d' size='340' side='right'caption='[[4x1d]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4x1d]] is a 2 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=4X1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X1D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4x1d]] 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=4X1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X1D FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x1b|4x1b]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene></td></tr>
-<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=4x1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x1d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x1d RCSB], [http://www.ebi.ac.uk/pdbsum/4x1d PDBsum]</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=4x1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x1d OCA], [https://pdbe.org/4x1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x1d RCSB], [https://www.ebi.ac.uk/pdbsum/4x1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x1d 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>
+[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 ==
-[[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.
+[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 ==
+X-ray crystal structures of human serum transferrin (77 kDa) with YbIII or FeIII bound to the C-lobe and malonate as the synergistic anion show that the large YbIII ion causes the expansion of the metal binding pocket while octahedral metal coordination geometry is preserved, an unusual geometry for a lanthanide ion.
+"Anion clamp" allows flexible protein to impose coordination geometry on metal ions.,Wang M, Lai TP, Wang L, Zhang H, Yang N, Sadler PJ, Sun H Chem Commun (Camb). 2015 Apr 9. PMID:25854324<ref>PMID:25854324</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4x1d" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transferrin 3D structures|Transferrin 3D structures]]
 == References ==
 <references/>
@@ Line 16: / Line 29: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Sun, H]]
+[[Category: Large Structures]]
-[[Category: Wang, M]]
+[[Category: Sun H]]
-[[Category: Zhang, H]]
+[[Category: Wang M]]
-[[Category: Ferric]]
+[[Category: Zhang H]]
-[[Category: Malonate]]
-[[Category: Metal transport]]
-[[Category: Transferrin]]
-[[Category: Ytterbium]]