5ytu
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==Structure of human SOD1 complexed with isoproteranol in C2221 space group== | ==Structure of human SOD1 complexed with isoproteranol in C2221 space group== | ||
| - | <StructureSection load='5ytu' size='340' side='right'caption='[[5ytu]]' scene=''> | + | <StructureSection load='5ytu' size='340' side='right'caption='[[5ytu]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YTU OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YTU FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5FW:ISOPRENALINE'>5FW</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=S4P:Dihydrogen+tetrasulfide'>S4P</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5ytu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ytu OCA], [https://pdbe.org/5ytu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ytu RCSB], [https://www.ebi.ac.uk/pdbsum/5ytu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ytu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cu/Zn superoxide dismutase-1 (SOD1) mutations are causative for a subset of amyotrophic lateral sclerosis (ALS) cases. These mutations lead to structural instability, aggregation and ultimately motor neuron death. We have determined crystal structures of SOD1 in complex with a naphthalene-catechol-linked compound which binds with low micro-molar affinity to a site important for oxidative damage-induced aggregation. SOD1 Trp32 oxidation is indeed significantly inhibited by ligand binding. Our work shows how compound linking can be applied successfully to ligand interactions on the SOD1 surface to generate relatively good binding strength. The ligand, positioned in a region important for SOD1 fibrillation, offers the possibility that it, or a similar compound, could prevent the abnormal self-association that drives SOD1 toxicity in ALS. | ||
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| + | Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation.,Manjula R, Wright GSA, Strange RW, Padmanabhan B FEBS Lett. 2018 May;592(10):1725-1737. doi: 10.1002/1873-3468.13055. Epub 2018, May 11. PMID:29679384<ref>PMID:29679384</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5ytu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of human SOD1 complexed with isoproteranol in C2221 space group
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