5j07 - Revision history

OCA at 10:40, 6 September 2023

OCA — Wed, 06 Sep 2023 10:40:45 GMT

←Older revision		Revision as of 10:40, 6 September 2023
Line 1:		Line 1:

	==Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1/2==		==Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1/2==
-	<StructureSection load='5j07' size='340' side='right' caption='[[5j07]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5j07' size='340' side='right'caption='[[5j07]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5j07]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J07 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5J07 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5j07]] 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=5J07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J07 FirstGlance]. <br>
-	</td></tr><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 HUMAN])~~</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]] 2Å</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=5j07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j07 OCA], [~~http~~://pdbe.org/5j07 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5j07 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5j07 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5j07 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=5j07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j07 OCA], [https://pdbe.org/5j07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j07 RCSB], [https://www.ebi.ac.uk/pdbsum/5j07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j07 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== 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>	+	[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 ==		== 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.	+	[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5j07" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5j07" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Superoxide dismutase 3D structures\|Superoxide dismutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Danielsson, J]]	+	[[Category: Large Structures]]
-	[[Category: Lang, L]]	+	[[Category: Danielsson J]]
-	[[Category: Logan, D]]	+	[[Category: Lang L]]
-	[[Category: Oliveberg, M]]	+	[[Category: Logan D]]
-	[[Category: Wang, H]]	+	[[Category: Oliveberg M]]
-	~~[[Category: Oxidoreductase]]~~	+	[[Category: Wang H]]
-	~~[[Category: Sod1~~]]	+

OCA at 08:07, 17 January 2018

OCA — Wed, 17 Jan 2018 08:07:14 GMT

←Older revision		Revision as of 08:07, 17 January 2018
Line 3:		Line 3:
	<StructureSection load='5j07' size='340' side='right' caption='[[5j07]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5j07' size='340' side='right' caption='[[5j07]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5j07]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J07 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5j07]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J07 FirstGlance]. <br>
-	</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=5j07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j07 OCA], [http://pdbe.org/5j07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j07 RCSB], [http://www.ebi.ac.uk/pdbsum/5j07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j07 ProSAT]</span></td></tr>	+	</td></tr><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 HUMAN])</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=5j07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j07 OCA], [http://pdbe.org/5j07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j07 RCSB], [http://www.ebi.ac.uk/pdbsum/5j07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j07 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Danielsson, J]]		[[Category: Danielsson, J]]
	[[Category: Lang, L]]		[[Category: Lang, L]]

OCA at 17:53, 1 February 2017

OCA — Wed, 01 Feb 2017 17:53:10 GMT

←Older revision		Revision as of 17:53, 1 February 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5j07 is ~~ON HOLD~~ ~~until Mar 27 2018~~	+	==Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1/2==
		+	<StructureSection load='5j07' size='340' side='right' caption='[[5j07]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5j07]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J07 FirstGlance]. <br>
		+	</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=5j07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j07 OCA], [http://pdbe.org/5j07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j07 RCSB], [http://www.ebi.ac.uk/pdbsum/5j07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j07 ProSAT]</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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Despite continuing interest in partly unfolded proteins as precursors for aggregation and adverse gain-of-function in human disease, there is yet little known about the local transitions of native structures that possibly lead to such intermediate states. To target this problem, we present here a protein-design strategy that allows real-time detection of rupture and swapping of complete secondary-structure elements in globular proteins-molecular events that have previously been inaccessible experimental analysis. The approach is applied to the dynamic beta-barrel of SOD1, associated with pathologic aggregation in the neurodegenerative disease ALS. Data show that rupture and re-insertion of individual beta-strands do not take place locally but require the SOD1 barrel to unfold globally. The finding questions the very existence of partly unfolded intermediates in the SOD1 aggregation process and presents new clues to the mechanism by which hydrogen bonding maintains global structural integrity.

-	~~Authors:~~ Wang, H., Lang, L., Logan~~, D.~~, Danielsson, J., Oliveberg, M.	+	Tricking a Protein To Swap Strands.,Wang H, Lang L, Logan DT, Danielsson J, Oliveberg M J Am Chem Soc. 2016 Dec 7;138(48):15571-15579. Epub 2016 Nov 22. PMID:27783493<ref>PMID:27783493</ref>

-	~~Description: Monomeric Human Cu~~,~~Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1~~/2	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
-	~~[[Category: Logan, D]]~~	+	<div class="pdbe-citations 5j07" style="background-color:#fffaf0;"></div>
-	~~[[Category: Oliveberg, M]]~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Danielsson, J]]		[[Category: Danielsson, J]]
	[[Category: Lang, L]]		[[Category: Lang, L]]
		+	[[Category: Logan, D]]
		+	[[Category: Oliveberg, M]]
	[[Category: Wang, H]]		[[Category: Wang, H]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Sod1]]

OCA: Protected "5j07" [edit=sysop:move=sysop]

OCA — Wed, 11 May 2016 01:14:55 GMT

Protected "5j07" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:14, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5j07 is ON HOLD until Mar 27 2018 Authors: Wang, H., Lang, L., Logan, D., Danielsson, J., Oliveberg, M. Description: Monomeric Human Cu,Zn Superoxi...

OCA — Wed, 11 May 2016 01:14:53 GMT

New page: '''Unreleased structure''' The entry 5j07 is ON HOLD until Mar 27 2018 Authors: Wang, H., Lang, L., Logan, D., Danielsson, J., Oliveberg, M. Description: Monomeric Human Cu,Zn Superoxi...

New page

'''Unreleased structure'''

The entry 5j07 is ON HOLD until Mar 27 2018

Authors: Wang, H., Lang, L., Logan, D., Danielsson, J., Oliveberg, M.

Description: Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1/2
[[Category: Unreleased Structures]]
[[Category: Logan, D]]
[[Category: Oliveberg, M]]
[[Category: Danielsson, J]]
[[Category: Lang, L]]
[[Category: Wang, H]]