5sve - Revision history

OCA at 12:48, 4 October 2023

OCA — Wed, 04 Oct 2023 12:48:21 GMT

←Older revision		Revision as of 12:48, 4 October 2023
Line 3:		Line 3:
	<StructureSection load='5sve' size='340' side='right'caption='[[5sve]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='5sve' size='340' side='right'caption='[[5sve]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5sve]] is a 3 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=5SVE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5SVE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5sve]] is a 3 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=5SVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SVE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=CA:CALCIUM+ION'>CA</scene~~>, ~~<scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 2.596Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~PPP3CA, CALNA, CNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN]), PPP3R1, CNA2, CNB ([http~~:~~//www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16]~~ </~~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=5sve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sve OCA], [https://pdbe.org/5sve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sve RCSB], [https://www.ebi.ac.uk/pdbsum/5sve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sve ProSAT]</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=5sve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sve OCA], [~~http~~://pdbe.org/5sve PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5sve RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5sve PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5sve ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN]] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref> ~~[[http://www.uniprot.org/uniprot/CANB1_HUMAN CANB1_HUMAN]] Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.~~	+	[https://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Phosphoprotein phosphatase]]~~	+	[[Category: Page R]]
-	[[Category: Page, R]]	+	[[Category: Peti W]]
-	[[Category: Peti, W]]	+	[[Category: Sheftic SR]]
-	[[Category: Sheftic~~, S R]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 08:57, 18 December 2019

OCA — Wed, 18 Dec 2019 08:57:21 GMT

←Older revision		Revision as of 08:57, 18 December 2019
Line 1:		Line 1:

	==Structure of Calcineurin in complex with NFATc1 LxVP peptide==		==Structure of Calcineurin in complex with NFATc1 LxVP peptide==
-	<StructureSection load='5sve' size='340' side='right' caption='[[5sve]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='5sve' size='340' side='right'caption='[[5sve]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5sve]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SVE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5sve]] is a 3 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=5SVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SVE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPP3CA, CALNA, CNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PPP3R1, CNA2, CNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=5sve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sve OCA], [http://pdbe.org/5sve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sve RCSB], [http://www.ebi.ac.uk/pdbsum/5sve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sve ProSAT]</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=5sve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sve OCA], [http://pdbe.org/5sve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sve RCSB], [http://www.ebi.ac.uk/pdbsum/5sve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sve ProSAT]</span></td></tr>
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5sve" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5sve" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calcineurin 3D structures\|Calcineurin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Phosphoprotein phosphatase]]		[[Category: Phosphoprotein phosphatase]]
	[[Category: Page, R]]		[[Category: Page, R]]

OCA at 18:50, 15 November 2017

OCA — Wed, 15 Nov 2017 18:50:12 GMT

←Older revision		Revision as of 18:50, 15 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5sve" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5sve" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Calcineurin\|Calcineurin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:31, 21 September 2017

OCA — Thu, 21 Sep 2017 04:31:49 GMT

←Older revision		Revision as of 04:31, 21 September 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5sve" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5sve" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calcineurin\|Calcineurin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:37, 18 January 2017

OCA — Wed, 18 Jan 2017 16:37:12 GMT

←Older revision		Revision as of 16:37, 18 January 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5sve is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Structure of Calcineurin in complex with NFATc1 LxVP peptide==
		+	<StructureSection load='5sve' size='340' side='right' caption='[[5sve]], [[Resolution\|resolution]] 2.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5sve]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SVE FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=5sve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sve OCA], [http://pdbe.org/5sve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sve RCSB], [http://www.ebi.ac.uk/pdbsum/5sve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sve ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN]] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref> [[http://www.uniprot.org/uniprot/CANB1_HUMAN CANB1_HUMAN]] Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ser/thr phosphorylation is the primary reversible covalent modification of proteins in eukaryotes. As a consequence, it is the reciprocal actions of kinases and phosphatases that act as key molecular switches to fine tune cellular events. It has been well documented that ~400 human ser/thr kinases engage substrates via consensus phosphosite sequences. Strikingly, we know comparatively little about the mechanism by which ~40 human protein ser/thr phosphatases (PSPs) dephosphorylate ~15000 different substrates with high specificity. The identification of substrates of the essential PSP calcineurin (CN) has been exceptionally challenging and only a small fraction has been biochemically confirmed. It is now emerging that CN binds regulators and substrates via two short linear motifs (SLiMs), the well-studied PxIxIT SLiM and the LxVP SLiM, which remains controversial at the molecular level. Here we describe the crystal structure of CN in complex with its substrate NFATc1 and show that the LxVP SLiM is correctly defined as piLxVP. Bioinformatics studies using the piLxVP SLiM resulted in the identification of 567 potential CN substrates; a small subset was experimentally confirmed. This combined structural-bioinformatics approach provides a powerful method for dissecting the CN interaction network and for elucidating the role of CN in human health and disease.

-	~~Authors: Sheftic, S.R~~., ~~Page~~, R., Peti, W.	+	Investigating the human Calcineurin Interaction Network using the piLxVP SLiM.,Sheftic SR, Page R, Peti W Sci Rep. 2016 Dec 15;6:38920. doi: 10.1038/srep38920. PMID:27974827<ref>PMID:27974827</ref>

-	~~Description: Structure~~ of ~~Calcineurin in complex with NFATc1 LxVP peptide~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5sve" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Phosphoprotein phosphatase]]
	[[Category: Page, R]]		[[Category: Page, R]]
-	[[Category: Sheftic, S.R]]
	[[Category: Peti, W]]		[[Category: Peti, W]]
		+	[[Category: Sheftic, S R]]
		+	[[Category: Hydrolase]]
		+	[[Category: Protein binding]]

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

OCA — Fri, 09 Sep 2016 15:19:07 GMT

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

←Older revision

Revision as of 15:19, 9 September 2016

OCA: New page: '''Unreleased structure''' The entry 5sve is ON HOLD until Paper Publication Authors: Sheftic, S.R., Page, R., Peti, W. Description: Structure of Calcineurin in complex with NFATc1 LxV...

OCA — Fri, 09 Sep 2016 15:19:06 GMT

New page: '''Unreleased structure''' The entry 5sve is ON HOLD until Paper Publication Authors: Sheftic, S.R., Page, R., Peti, W. Description: Structure of Calcineurin in complex with NFATc1 LxV...

New page

'''Unreleased structure'''

The entry 5sve is ON HOLD until Paper Publication

Authors: Sheftic, S.R., Page, R., Peti, W.

Description: Structure of Calcineurin in complex with NFATc1 LxVP peptide
[[Category: Unreleased Structures]]
[[Category: Page, R]]
[[Category: Sheftic, S.R]]
[[Category: Peti, W]]