5n0k
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Rat ceruloplasmin orthorhombic form== | |
| + | <StructureSection load='5n0k' size='340' side='right' caption='[[5n0k]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5n0k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N0K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N0K FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n0k OCA], [http://pdbe.org/5n0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n0k RCSB], [http://www.ebi.ac.uk/pdbsum/5n0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n0k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. The structural organization of Cp causes its sensitivity to proteolysis and ROS (reactive oxygen species), which can alter some of the important Cp functions. Elucidation of the orthorhombic crystal structure of rat Cp at 2.3 A resolution revealed the basis for stronger resistance of rat Cp to proteolysis and a new labile copper binding site. The presence of this site appears as a very rare and distinctive feature of rat Cp as was shown by sequence alignment of ceruloplasmin, hephaestin and zyklopen in the Deuterostomia taxonomic group. The trigonal crystal form of rat Cp at 3.2 A demonstrates unexpected partial substitution of copper by zinc. | ||
| - | + | Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic.,Samygina VR, Sokolov AV, Bourenkov G, Schneider TR, Anashkin VA, Kozlov SO, Kolmakov NN, Vasilyev VB Metallomics. 2017 Nov 27. doi: 10.1039/c7mt00157f. PMID:29177316<ref>PMID:29177316</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5n0k" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Rattus norvegicus]] | ||
[[Category: Bourenkov, G]] | [[Category: Bourenkov, G]] | ||
| - | [[Category: | + | [[Category: Samygina, V R]] |
| - | [[Category: | + | [[Category: Sokolov, A V]] |
| + | [[Category: Vasilyev, V B]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 06:54, 13 December 2017
Rat ceruloplasmin orthorhombic form
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