4dat - Revision history

OCA at 09:55, 30 October 2024

2024-10-30T09:55:29Z

← Older revision		Revision as of 09:55, 30 October 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dat]] 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=4DAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DAT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dat]] 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=4DAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DAT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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]] 1.4Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=4dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dat OCA], [https://pdbe.org/4dat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dat RCSB], [https://www.ebi.ac.uk/pdbsum/4dat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dat 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=4dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dat OCA], [https://pdbe.org/4dat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dat RCSB], [https://www.ebi.ac.uk/pdbsum/4dat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dat ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/1433S_HUMAN 1433S_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.		[https://www.uniprot.org/uniprot/1433S_HUMAN 1433S_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 08:09, 21 September 2022

2022-09-21T08:09:20Z

← Older revision		Revision as of 08:09, 21 September 2022
Line 1:		Line 1:

	==Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II==		==Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II==
	<StructureSection load='4dat' size='340' side='right' caption='[[4dat]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='4dat' size='340' side='right'caption='[[4dat]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dat]] 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=4DAT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DAT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dat]] 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=4DAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DAT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=4dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dat OCA], [https://pdbe.org/4dat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dat RCSB], [https://www.ebi.ac.uk/pdbsum/4dat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dat ProSAT]</span></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yz5\|1yz5]], [[4dau\|4dau]]</td></tr>~~
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFN, HME1 ([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/Protein-arginine_deiminase Protein-arginine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.15 3.5.3.15] </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=4dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dat OCA], [~~http~~://pdbe.org/4dat PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dat RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dat PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dat ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/1433S_HUMAN 1433S_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression. [[http://www.uniprot.org/uniprot/PADI6_HUMAN PADI6_HUMAN]] Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity).		[[https://www.uniprot.org/uniprot/1433S_HUMAN 1433S_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 20:

	==See Also==		==See Also==
	*[[14-3-3 protein\|14-3-3 protein]]		*[[14-3-3 protein 3D structures\|14-3-3 protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Protein-arginine deiminase~~]]		[[Category: Large Structures]]
	[[Category: Ottmann, C]]		[[Category: Ottmann C]]
	[[Category: Rose, M]]		[[Category: Rose M]]
	[[Category: Rose, R]]		[[Category: Rose R]]
	~~[[Category: 14-3-3 fold]]~~
	~~[[Category: Protein-protein interaction]]~~
	~~[[Category: Signaling protein-protein binding complex~~]]

OCA at 18:53, 4 August 2016

2016-08-04T18:53:18Z

← Older revision		Revision as of 18:53, 4 August 2016
Line 1:		Line 1:

	==Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II==		==Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II==
	<StructureSection load='4dat' size='340' side='right' caption='[[4dat]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='4dat' size='340' side='right' caption='[[4dat]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dat]] 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=4DAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dat]] 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=4DAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yz5\|1yz5]], [[4dau\|4dau]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yz5\|1yz5]], [[4dau\|4dau]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFN, HME1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFN, HME1 ([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/Protein-arginine_deiminase Protein-arginine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.15 3.5.3.15] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-arginine_deiminase Protein-arginine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.15 3.5.3.15] </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=4dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dat OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dat RCSB], [http://www.ebi.ac.uk/pdbsum/4dat PDBsum]</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=4dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dat OCA], [http://pdbe.org/4dat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dat RCSB], [http://www.ebi.ac.uk/pdbsum/4dat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dat ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/1433S_HUMAN 1433S_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression. [[http://www.uniprot.org/uniprot/~~Q330K5_HUMAN Q330K5_HUMAN~~]] Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity).		[[http://www.uniprot.org/uniprot/1433S_HUMAN 1433S_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression. [[http://www.uniprot.org/uniprot/PADI6_HUMAN PADI6_HUMAN]] Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 21:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4dat" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Protein-arginine deiminase]]		[[Category: Protein-arginine deiminase]]
	[[Category: Ottmann, C]]		[[Category: Ottmann, C]]

OCA at 12:08, 25 December 2014

2014-12-25T12:08:43Z

← Older revision		Revision as of 12:08, 25 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4dat~~.~~png~~\|~~left~~\|~~200px~~]]		==Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II==
			<StructureSection load='4dat' size='340' side='right' caption='[[4dat]], [[Resolution\|resolution]] 1.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4dat]] 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=4DAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DAT FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
			<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yz5\|1yz5]], [[4dau\|4dau]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFN, HME1 ([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/Protein-arginine_deiminase Protein-arginine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.15 3.5.3.15] </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=4dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dat OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dat RCSB], [http://www.ebi.ac.uk/pdbsum/4dat PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/1433S_HUMAN 1433S_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression. [[http://www.uniprot.org/uniprot/Q330K5_HUMAN Q330K5_HUMAN]] Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity).
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The regulation and function of peptidylarginine deiminase isoform VI (PAD6), which is a highly abundant protein associated with the cytoplasmic lattices in mammalian oocytes, is poorly understood so far. It has been shown previously, that 14-3-3 proteins, a class of regulatory adapter proteins ubiquitous in eukaryotes, bind to PAD6 in vivo in a phosphorylation dependant manner. Here we identify possible 14-3-3 binding sites in human PAD6 by in silico methods, looking for conserved, surface exposed serine residues. Two of these sites were confirmed as 14-3-3 binding sites by fluorescence polarization competition and X-ray crystallography. We furthermore suggest a role of RSK-type kinases in the phosphorylation of one of these two binding sites and provide evidence in the form of in vitro kinase assays with p70S6 kinase and RSK1.

	~~{{STRUCTURE_4dat\| PDB=4dat \| SCENE= }}~~		Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI.,Rose R, Rose M, Ottmann C J Struct Biol. 2012 May 24. PMID:22634725<ref>PMID:22634725</ref>

	~~===Structure~~ of ~~14-3-3 sigma in complex with PADI6 14-3-3 binding motif II===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_22634725}}~~		==See Also==
			*[[14-3-3 protein\|14-3-3 protein]]
	==~~About this Structure~~==		== References ==
	[[~~4dat~~]] 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=4DAT OCA].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:022634725<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein-arginine deiminase]]		[[Category: Protein-arginine deiminase]]
	[[Category: Ottmann, C.]]		[[Category: Ottmann, C]]
	[[Category: Rose, M.]]		[[Category: Rose, M]]
	[[Category: Rose, R.]]		[[Category: Rose, R]]
	[[Category: 14-3-3 fold]]		[[Category: 14-3-3 fold]]
	[[Category: Protein-protein interaction]]		[[Category: Protein-protein interaction]]
	[[Category: Signaling protein-protein binding complex]]		[[Category: Signaling protein-protein binding complex]]

OCA at 06:31, 24 October 2012

2012-10-24T06:31:15Z

← Older revision		Revision as of 06:31, 24 October 2012
Line 1:		Line 1:
	[[Image:4dat.~~jpg~~\|left\|200px]]		[[Image:4dat.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_4dat", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_4dat\| PDB=4dat \| SCENE= }}		{{STRUCTURE_4dat\| PDB=4dat \| SCENE= }}

	===Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II===		===Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_22634725}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 22634725 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_22634725}}		{{ABSTRACT_PUBMED_22634725}}

OCA at 06:12, 13 June 2012

2012-06-13T06:12:41Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4dat.jpg|left|200px]]
-The entry 4dat is ON HOLD  until Paper Publication
+<!--
-Authors: Rose, R., Rose, M., Ottmann, C.
+===Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II===
-Description: Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II

OCA at 06:09, 8 February 2012

2012-02-08T06:09:47Z

← Older revision		Revision as of 06:09, 8 February 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4dat is ON HOLD		The entry 4dat is ON HOLD until Paper Publication

	Authors: Rose, R., Rose, M., Ottmann, C.		Authors: Rose, R., Rose, M., Ottmann, C.

	Description: Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II		Description: Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II

OCA: Protected "4dat" [edit=sysop:move=sysop]

2012-01-25T06:09:53Z

Protected "4dat" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:09, 25 January 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4dat is ON HOLD Authors: Rose, R., Rose, M., Ottmann, C. Description: Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II

2012-01-25T06:09:49Z

New page: '''Unreleased structure''' The entry 4dat is ON HOLD Authors: Rose, R., Rose, M., Ottmann, C. Description: Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II

New page

'''Unreleased structure'''

The entry 4dat is ON HOLD

Authors: Rose, R., Rose, M., Ottmann, C.

Description: Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif II