2wz0

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[[Image:2wz0.png|left|200px]]
 
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{{STRUCTURE_2wz0| PDB=2wz0 | SCENE= }}
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==L38V SOD1 mutant complexed with aniline.==
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<StructureSection load='2wz0' size='340' side='right'caption='[[2wz0]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2wz0]] 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=2WZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WZ0 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZZT:2-METHOXY-5-METHYLANILINE'>ZZT</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wz0 OCA], [https://pdbe.org/2wz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wz0 RCSB], [https://www.ebi.ac.uk/pdbsum/2wz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wz0 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[https://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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[https://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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Dominant inheritance of point mutations in CuZn superoxide dismutase (SOD1) is the best characterized subset of familial amyotrophic lateral sclerosis (FALS) and accounts for some 20% of the known familial cases. We report the discovery and visualization via cocrystallography of two ligand-binding pockets in human SOD1 and its pathogenic mutants that have opened up the real possibility of undertaking lead compound discovery using a fragment-based approach for therapeutic purposes for SOD1 associated motor neuron disease.
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===L38V SOD1 MUTANT COMPLEXED WITH ANILINE.===
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Structural discovery of small molecule binding sites in Cu-Zn human superoxide dismutase familial amyotrophic lateral sclerosis mutants provides insights for lead optimization.,Antonyuk S, Strange RW, Hasnain SS J Med Chem. 2010 Feb 11;53(3):1402-6. PMID:20067275<ref>PMID:20067275</ref>
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{{ABSTRACT_PUBMED_20067275}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2wz0" style="background-color:#fffaf0;"></div>
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[[2wz0]] 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=2WZ0 OCA].
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==See Also==
==See Also==
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*[[Superoxide Dismutase|Superoxide Dismutase]]
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:020067275</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Superoxide dismutase]]
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[[Category: Large Structures]]
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[[Category: Antonyuk, S.]]
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[[Category: Antonyuk S]]
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[[Category: Hasnain, S S.]]
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[[Category: Hasnain SS]]
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[[Category: Strange, R W.]]
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[[Category: Strange RW]]
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[[Category: Amyotrophic lateral sclerosis]]
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[[Category: Antioxidant]]
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[[Category: Disease mutation]]
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[[Category: Oxidoreductase]]
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Current revision

L38V SOD1 mutant complexed with aniline.

PDB ID 2wz0

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Proteopedia Page Contributors and Editors (what is this?)

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