7fb6 - Revision history

OCA at 17:12, 29 November 2023

2023-11-29T17:12:40Z

←Older revision		Revision as of 17:12, 29 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7fb6]] 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=7FB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FB6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[7fb6]] 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=7FB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FB6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.8Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=7fb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fb6 OCA], [https://pdbe.org/7fb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fb6 RCSB], [https://www.ebi.ac.uk/pdbsum/7fb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fb6 ProSAT]</span></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=7fb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fb6 OCA], [https://pdbe.org/7fb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fb6 RCSB], [https://www.ebi.ac.uk/pdbsum/7fb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fb6 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:22, 26 October 2022

2022-10-26T06:22:37Z

←Older revision		Revision as of 06:22, 26 October 2022
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-	'''Unreleased structure'''

-	~~The entry~~ 7fb6 is ~~ON HOLD until 2023~~-10-08	+	==C57D/C146D mutant of Human Cu, Zn Superoxide Dismutase (SOD1)==
		+	<StructureSection load='7fb6' size='340' side='right'caption='[[7fb6]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[7fb6]] 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=7FB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FB6 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=7fb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fb6 OCA], [https://pdbe.org/7fb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fb6 RCSB], [https://www.ebi.ac.uk/pdbsum/7fb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fb6 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[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>
		+	== Function ==
		+	[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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Eukaryotic Cu, Zn-superoxide dismutase (SOD1) is primarily responsible for cytotoxic filament formation in amyotrophic lateral sclerosis (ALS) neurons. Two cysteine residues in SOD1 form an intramolecular disulfide bond. This study aims to explore the molecular mechanism of SOD1 filament formation by cysteine overoxidation in sporadic ALS (sALS). In this study, we determined the crystal structure of the double mutant (C57D/C146D) SOD1 that mimics the overoxidation of the disulfide-forming cysteine residues. The structure revealed the open and relaxed conformation of loop IV containing the mutated Asp57. The double mutant SOD1 produced more contagious filaments than wild-type protein, promoting filament formation of the wild-type SOD1 proteins. Importantly, we further found that HOCl treatment to the wild-type SOD1 proteins facilitated their filament formation. We propose a feasible mechanism for SOD1 filament formation in ALS from the wild-type SOD1, suggesting that overoxidized SOD1 is a triggering factor of sALS. Our findings extend our understanding of other neurodegenerative disorders associated with ROS stresses at the molecular level.

-	~~Authors~~:	+	Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation.,Baek Y, Woo TG, Ahn J, Lee D, Kwon Y, Park BJ, Ha NC Commun Biol. 2022 Oct 12;5(1):1085. doi: 10.1038/s42003-022-04017-0. PMID:36224351<ref>PMID:36224351</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 7fb6" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Baek Y]]
		+	[[Category: Ha N-C]]

OCA at 06:00, 29 June 2022

2022-06-29T06:00:51Z

←Older revision		Revision as of 06:00, 29 June 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7fb6 is ON HOLD	+	The entry 7fb6 is ON HOLD until 2023-10-08

	Authors:		Authors:

OCA at 06:20, 22 June 2022

2022-06-22T06:20:47Z

←Older revision		Revision as of 06:20, 22 June 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7fb6 is ON HOLD ~~until Oct 08 2023~~	+	The entry 7fb6 is ON HOLD

	Authors:		Authors:

OCA at 03:48, 15 June 2022

2022-06-15T03:48:26Z

←Older revision		Revision as of 03:48, 15 June 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7fb6 is ON HOLD until ~~Paper Publication~~	+	The entry 7fb6 is ON HOLD until Oct 08 2023

	Authors:		Authors:

OCA at 11:41, 29 December 2021

2021-12-29T11:41:23Z

←Older revision		Revision as of 11:41, 29 December 2021
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7fb6 is ON HOLD	+	The entry 7fb6 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7fb6" [edit=sysop:move=sysop]

2021-07-14T08:44:04Z

Protected "7fb6" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:44, 14 July 2021

OCA: New page: '''Unreleased structure''' The entry 7fb6 is ON HOLD Authors: Description: Category: Unreleased Structures

2021-07-14T08:44:03Z

New page: '''Unreleased structure''' The entry 7fb6 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7fb6 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]