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4ejx
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4ejx is ON HOLD Authors: Valeriya R. Samygina, Alexey V. Sokolov, Gleb Bourenkov, Vadim B. Vasilyev, Hans Bartunik Description: Structure of cerulo...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of ceruloplasmin-myeloperoxidase complex== | |
| + | <StructureSection load='4ejx' size='340' side='right'caption='[[4ejx]], [[Resolution|resolution]] 4.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ejx]] is a 3 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=4EJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EJX 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]] 4.69Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4ejx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ejx OCA], [https://pdbe.org/4ejx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ejx RCSB], [https://www.ebi.ac.uk/pdbsum/4ejx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ejx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[https://omim.org/entry/604290 604290]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). | ||
| - | + | ==See Also== | |
| - | + | *[[Ceruloplasmin|Ceruloplasmin]] | |
| - | + | *[[Myeloperoxidase|Myeloperoxidase]] | |
| + | *[[Sandbox WWC11|Sandbox WWC11]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bartunik H]] | ||
| + | [[Category: Bourenkov G]] | ||
| + | [[Category: Samygina VR]] | ||
| + | [[Category: Sokolov AV]] | ||
| + | [[Category: Vasilyev VB]] | ||
Current revision
Structure of ceruloplasmin-myeloperoxidase complex
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