1a37 - Revision history

OCA at 15:20, 13 March 2024

OCA — Wed, 13 Mar 2024 15:20:52 GMT

←Older revision		Revision as of 15:20, 13 March 2024
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	<StructureSection load='1a37' size='340' side='right'caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1a37' size='340' side='right'caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bovin Bovin~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A37 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A37 FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.6Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [https://pdbe.org/1a37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [https://www.ebi.ac.uk/pdbsum/1a37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a37 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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [https://pdbe.org/1a37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [https://www.ebi.ac.uk/pdbsum/1a37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a37 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN]] 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. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.<ref>PMID:7931346</ref>	+	[https://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN] 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. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.<ref>PMID:7931346</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</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/main_output.php?pdb_ID=1a37 ConSurf].		</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/main_output.php?pdb_ID=1a37 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	14-3-3 proteins bind a variety of molecules involved in signal transduction, cell cycle regulation and apoptosis. 14-3-3 binds ligands such as Raf-1 kinase and Bad by recognizing the phosphorylated consensus motif, RSXpSXP, but must bind unphosphorylated ligands, such as glycoprotein Ib and Pseudomonas aeruginosa exoenzyme S, via a different motif. Here we report the crystal structures of the zeta isoform of 14-3-3 in complex with two peptide ligands: a Raf-derived phosphopeptide (pS-Raf-259, LSQRQRSTpSTPNVHMV) and an unphosphorylated peptide derived from phage display (R18, PHCVPRDLSWLDLEANMCLP) that inhibits binding of exoenzyme S and Raf-1. The two peptides bind within a conserved amphipathic groove on the surface of 14-3-3 at overlapping but distinct sites. The phosphoserine of pS-Raf-259 engages a cluster of basic residues (Lys49, Arg56, Arg60, and Arg127), whereas R18 binds via the amphipathic sequence, WLDLE, with its two acidic groups coordinating the same basic cluster. 14-3-3 is dimeric, and its two peptide-binding grooves are arranged in an antiparallel fashion, 30 A apart. The ability of each groove to bind different peptide motifs suggests how 14-3-3 can act in signal transduction by inducing either homodimer or heterodimer formation in its target proteins.
-
-	14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove.,Petosa C, Masters SC, Bankston LA, Pohl J, Wang B, Fu H, Liddington RC J Biol Chem. 1998 Jun 26;273(26):16305-10. PMID:9632691<ref>PMID:9632691</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1a37" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bovin~~]]	+	[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fu, H]]	+	[[Category: Fu H]]
-	[[Category: Liddington~~, R C~~]]	+	[[Category: Liddington RC]]
-	[[Category: Masters~~, S C~~]]	+	[[Category: Masters SC]]
-	[[Category: Petosa, C]]	+	[[Category: Petosa C]]
-	[[Category: Pohl, J]]	+	[[Category: Pohl J]]
-	[[Category: Wang, B]]	+	[[Category: Wang B]]
-	~~[[Category: Signal transduction~~]]	+

OCA at 15:51, 22 December 2021

OCA — Wed, 22 Dec 2021 15:51:27 GMT

←Older revision		Revision as of 15:51, 22 December 2021
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	<StructureSection load='1a37' size='340' side='right'caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1a37' size='340' side='right'caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1A37 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A37 FirstGlance]. <br>
	</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>		</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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [~~http~~://pdbe.org/1a37 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1a37 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1a37 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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [https://pdbe.org/1a37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [https://www.ebi.ac.uk/pdbsum/1a37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a37 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN]] 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. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.<ref>PMID:7931346</ref>	+	[[https://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN]] 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. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.<ref>PMID:7931346</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:36, 18 March 2020

OCA — Wed, 18 Mar 2020 10:36:29 GMT

←Older revision		Revision as of 10:36, 18 March 2020
Line 1:		Line 1:

	==14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE==		==14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE==
-	<StructureSection load='1a37' size='340' side='right' caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>	+	<StructureSection load='1a37' size='340' side='right'caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>
Line 30:		Line 30:

	==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/>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Bovin]]		[[Category: Bovin]]
		+	[[Category: Large Structures]]
	[[Category: Fu, H]]		[[Category: Fu, H]]
	[[Category: Liddington, R C]]		[[Category: Liddington, R C]]

OCA at 08:41, 14 June 2018

OCA — Thu, 14 Jun 2018 08:41:06 GMT

←Older revision		Revision as of 08:41, 14 June 2018
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a3/1a37_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a3/1a37_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 04:50, 9 September 2016

OCA — Fri, 09 Sep 2016 04:50:37 GMT

←Older revision		Revision as of 04:50, 9 September 2016
Line 1:		Line 1:
		+
	==14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE==		==14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE==
	<StructureSection load='1a37' size='340' side='right' caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1a37' size='340' side='right' caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>
-	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~PSE~~:~~O-PHOSPHOETHANOLAMINE~~'>~~PSE~~</scene></td></tr>	+	</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://pdbe.org/1a37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://pdbe.org/1a37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a37 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 14:46, 9 February 2016

OCA — Tue, 09 Feb 2016 14:46:22 GMT

←Older revision		Revision as of 14:46, 9 February 2016
Line 16:		Line 16:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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].	+	</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/main_output.php?pdb_ID=1a37 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:56, 9 September 2015

OCA — Wed, 09 Sep 2015 15:56:07 GMT

←Older revision		Revision as of 15:56, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1a37' size='340' side='right' caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1a37' size='340' side='right' caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bos_taurus Bos taurus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene></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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://pdbe.org/1a37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1a37" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bos taurus~~]]	+	[[Category: Bovin]]
	[[Category: Fu, H]]		[[Category: Fu, H]]
	[[Category: Liddington, R C]]		[[Category: Liddington, R C]]

OCA at 07:28, 25 December 2014

OCA — Thu, 25 Dec 2014 07:28:34 GMT

←Older revision		Revision as of 07:28, 25 December 2014
Line 6:		Line 6:
	<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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN]] 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. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.<ref>PMID:7931346</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:45, 22 December 2014

OCA — Mon, 22 Dec 2014 09:45:21 GMT

←Older revision		Revision as of 09:45, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 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=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Fu, H.]]	+	[[Category: Fu, H]]
-	[[Category: Liddington, R C.]]	+	[[Category: Liddington, R C]]
-	[[Category: Masters, S C.]]	+	[[Category: Masters, S C]]
-	[[Category: Petosa, C.]]	+	[[Category: Petosa, C]]
-	[[Category: Pohl, J.]]	+	[[Category: Pohl, J]]
-	[[Category: Wang, B.]]	+	[[Category: Wang, B]]
	[[Category: Signal transduction]]		[[Category: Signal transduction]]

OCA at 08:53, 3 October 2014

OCA — Fri, 03 Oct 2014 08:53:00 GMT

←Older revision		Revision as of 08:53, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1a37\| PDB=1a37 \| SCENE= }}~~	+	==14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE==
-	===14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE===	+	<StructureSection load='1a37' size='340' side='right' caption='[[1a37]], [[Resolution\|resolution]] 3.60Å' scene=''>
-	~~{{ABSTRACT_PUBMED_9632691}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1a37]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A37 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a37 RCSB], [http://www.ebi.ac.uk/pdbsum/1a37 PDBsum]</span></td></tr>
		+	<table>
		+	== 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/a3/1a37_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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	14-3-3 proteins bind a variety of molecules involved in signal transduction, cell cycle regulation and apoptosis. 14-3-3 binds ligands such as Raf-1 kinase and Bad by recognizing the phosphorylated consensus motif, RSXpSXP, but must bind unphosphorylated ligands, such as glycoprotein Ib and Pseudomonas aeruginosa exoenzyme S, via a different motif. Here we report the crystal structures of the zeta isoform of 14-3-3 in complex with two peptide ligands: a Raf-derived phosphopeptide (pS-Raf-259, LSQRQRSTpSTPNVHMV) and an unphosphorylated peptide derived from phage display (R18, PHCVPRDLSWLDLEANMCLP) that inhibits binding of exoenzyme S and Raf-1. The two peptides bind within a conserved amphipathic groove on the surface of 14-3-3 at overlapping but distinct sites. The phosphoserine of pS-Raf-259 engages a cluster of basic residues (Lys49, Arg56, Arg60, and Arg127), whereas R18 binds via the amphipathic sequence, WLDLE, with its two acidic groups coordinating the same basic cluster. 14-3-3 is dimeric, and its two peptide-binding grooves are arranged in an antiparallel fashion, 30 A apart. The ability of each groove to bind different peptide motifs suggests how 14-3-3 can act in signal transduction by inducing either homodimer or heterodimer formation in its target proteins.

-	~~==Function==~~	+	14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove.,Petosa C, Masters SC, Bankston LA, Pohl J, Wang B, Fu H, Liddington RC J Biol Chem. 1998 Jun 26;273(26):16305-10. PMID:9632691<ref>PMID:9632691</ref>
-	~~[[http://www.uniprot.org/uniprot/1433Z_BOVIN 1433Z_BOVIN]] 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~~. ~~Activates the ADP-ribosyltransferase~~ (~~exoS~~) ~~activity of bacterial origin~~.<ref>PMID:~~7931346~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[1a37]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bos_taurus Bos taurus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1A37 OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:009632691</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[14-3-3 protein\|14-3-3 protein]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Fu, H.]]		[[Category: Fu, H.]]