3h2q
From Proteopedia
(Difference between revisions)
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- | + | ==Human SOD1 H80R variant, P21 crystal form== | |
- | === | + | <StructureSection load='3h2q' size='340' side='right' caption='[[3h2q]], [[Resolution|resolution]] 1.85Å' scene=''> |
- | + | == Structural highlights == | |
- | ==Disease== | + | <table><tr><td colspan='2'>[[3h2q]] is a 4 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=3H2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H2Q FirstGlance]. <br> |
- | [[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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h2p|3h2p]], [[3h2r|3h2r]]</td></tr> | |
- | ==Function== | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
+ | <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> | ||
+ | <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=3h2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h2q RCSB], [http://www.ebi.ac.uk/pdbsum/3h2q PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [[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> | ||
+ | == Function == | ||
[[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. | [[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. | ||
- | + | == Evolutionary Conservation == | |
- | == | + | [[Image:Consurf_key_small.gif|200px|right]] |
- | [[ | + | Check<jmol> |
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/3h2q_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Superoxide Dismutase|Superoxide Dismutase]] | *[[Superoxide Dismutase|Superoxide Dismutase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | <references | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
- | [[Category: Cao, X | + | [[Category: Cao, X]] |
- | [[Category: Carroll, M C | + | [[Category: Carroll, M C]] |
- | [[Category: Culotta, V C | + | [[Category: Culotta, V C]] |
- | [[Category: Doucette, P A | + | [[Category: Doucette, P A]] |
- | [[Category: Hart, P J | + | [[Category: Hart, P J]] |
- | [[Category: Seetharaman, S V | + | [[Category: Seetharaman, S V]] |
- | [[Category: Taylor, A B | + | [[Category: Taylor, A B]] |
- | [[Category: Valentine, J S | + | [[Category: Valentine, J S]] |
- | [[Category: Whitson, L J | + | [[Category: Whitson, L J]] |
- | [[Category: Winkler, D D | + | [[Category: Winkler, D D]] |
[[Category: Amyotrophic lateral sclerosis]] | [[Category: Amyotrophic lateral sclerosis]] | ||
[[Category: Antioxidant]] | [[Category: Antioxidant]] |
Revision as of 17:22, 18 December 2014
Human SOD1 H80R variant, P21 crystal form
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Categories: Homo sapiens | Superoxide dismutase | Cao, X | Carroll, M C | Culotta, V C | Doucette, P A | Hart, P J | Seetharaman, S V | Taylor, A B | Valentine, J S | Whitson, L J | Winkler, D D | Amyotrophic lateral sclerosis | Antioxidant | Disease mutation | Disulfide bond | Human cu | Metal-binding | Oxidoreductase | Phosphoprotein | Zn superoxide dismutase