5wor

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'''Unreleased structure'''
 
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The entry 5wor is ON HOLD until Paper Publication
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==Corkscrew assembly of SOD1 residues 28-38 with familial mutation G37R==
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<StructureSection load='5wor' size='340' side='right' caption='[[5wor]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5wor]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WOR FirstGlance]. <br>
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</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></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
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<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=5wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wor OCA], [http://pdbe.org/5wor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wor RCSB], [http://www.ebi.ac.uk/pdbsum/5wor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wor ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[http://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The aggregation cascade of disease-related amyloidogenic proteins, terminating in insoluble amyloid fibrils, involves intermediate oligomeric states. The structural and biochemical details of these oligomers have been largely unknown. Here we report crystal structures of variants of the cytotoxic oligomer-forming segment residues 28-38 of the ALS-linked protein, SOD1. The crystal structures reveal three different architectures: corkscrew oligomeric structure, nontwisting curved sheet structure and a steric zipper proto-filament structure. Our work highlights the polymorphism of the segment 28-38 of SOD1 and identifies the molecular features of amyloidogenic entities.
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Authors: Sangwan, S., Sawaya, M.R., Eisenberg, D.S.
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Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations.,Sangwan S, Sawaya MR, Murray KA, Hughes MP, Eisenberg DS Protein Sci. 2018 Feb 17. doi: 10.1002/pro.3391. PMID:29453800<ref>PMID:29453800</ref>
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Description: Corkscrew assembly of SOD1 residues 28-38 with familial mutation G37R
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Eisenberg, D.S]]
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<div class="pdbe-citations 5wor" style="background-color:#fffaf0;"></div>
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[[Category: Sawaya, M.R]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Superoxide dismutase]]
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[[Category: Eisenberg, D S]]
[[Category: Sangwan, S]]
[[Category: Sangwan, S]]
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[[Category: Sawaya, M R]]
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[[Category: Amyloid-related oligomer]]
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[[Category: Protein fibril]]

Revision as of 05:28, 30 May 2018

Corkscrew assembly of SOD1 residues 28-38 with familial mutation G37R

5wor, resolution 2.77Å

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