5d2d - Revision history

OCA at 10:18, 21 June 2023

2023-06-21T10:18:59Z

←Older revision		Revision as of 10:18, 21 June 2023
Line 3:		Line 3:
	<StructureSection load='5d2d' size='340' side='right'caption='[[5d2d]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='5d2d' size='340' side='right'caption='[[5d2d]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5d2d]] 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=5D2D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5D2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5d2d]] 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=5D2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D2D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=~~SUC~~:~~SUCROSE~~'>~~SUC~~</scene><~~/td></tr>~~	+	</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=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</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=5d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2d OCA], [https://pdbe.org/5d2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d2d RCSB], [https://www.ebi.ac.uk/pdbsum/5d2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2d ProSAT]</span></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">YWHAZ ([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/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </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=5d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2d OCA], [~~http~~://pdbe.org/5d2d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5d2d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5d2d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2d ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[http://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[http://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_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.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref> [[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>	+	[https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_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.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Channel-conductance-controlling ATPase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Leysen~~, S F.R~~]]	+	[[Category: Leysen SFR]]
-	[[Category: Ottmann, C]]	+	[[Category: Ottmann C]]
-	[[Category: Stevers~~, L M]]~~	+	[[Category: Stevers LM]]
-	~~[[Category: Peptide binding protein]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Protein-peptide complex]]~~	+
-	~~[[Category: Tandem binding~~]]	+

OCA at 10:34, 1 April 2020

2020-04-01T10:34:05Z

←Older revision		Revision as of 10:34, 1 April 2020
Line 1:		Line 1:

	==Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768==		==Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768==
-	<StructureSection load='5d2d' size='340' side='right' caption='[[5d2d]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='5d2d' size='340' side='right'caption='[[5d2d]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5d2d]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5d2d]] 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=5D2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2D FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">YWHAZ ([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/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </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=5d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2d OCA], [http://pdbe.org/5d2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2d RCSB], [http://www.ebi.ac.uk/pdbsum/5d2d 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=5d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2d OCA], [http://pdbe.org/5d2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2d RCSB], [http://www.ebi.ac.uk/pdbsum/5d2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 22:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 5d2d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5d2d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[14-3-3 protein 3D structures\|14-3-3 protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Channel-conductance-controlling ATPase]]		[[Category: Channel-conductance-controlling ATPase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Leysen, S F.R]]		[[Category: Leysen, S F.R]]
	[[Category: Ottmann, C]]		[[Category: Ottmann, C]]

OCA at 03:47, 11 May 2016

2016-05-11T03:47:17Z

←Older revision		Revision as of 03:47, 11 May 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5d2d is ~~ON HOLD~~	+	==Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768==
		+	<StructureSection load='5d2d' size='340' side='right' caption='[[5d2d]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5d2d]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2D FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </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=5d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2d OCA], [http://pdbe.org/5d2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2d RCSB], [http://www.ebi.ac.uk/pdbsum/5d2d PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[http://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[http://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_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.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref> [[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cystic fibrosis is a fatal genetic disease, most frequently caused by the retention of the CFTR (cystic fibrosis transmembrane conductance regulator) mutant protein in the endoplasmic reticulum (ER). The binding of the 14-3-3 protein to the CFTR regulatory (R) domain has been found to enhance CFTR trafficking to the plasma membrane. To define the mechanism of action of this protein-protein interaction, we have examined the interaction in vitro. The disordered multiphosphorylated R domain contains nine different 14-3-3 binding motifs. Furthermore, the 14-3-3 protein forms a dimer containing two amphipathic grooves that can potentially bind these phosphorylated motifs. This results in a number of possible binding mechanisms between these two proteins. Using multiple biochemical assays and crystal structures, we show that the interaction between them is governed by two binding sites: The key binding site of CFTR (pS768) occupies one groove of the 14-3-3 dimer, and a weaker, secondary binding site occupies the other binding groove. We show that fusicoccin-A, a natural-product tool compound used in studies of 14-3-3 biology, can stabilize the interaction between 14-3-3 and CFTR by selectively interacting with a secondary binding motif of CFTR (pS753). The stabilization of this interaction stimulates the trafficking of mutant CFTR to the plasma membrane. This definition of the druggability of the 14-3-3-CFTR interface might offer an approach for cystic fibrosis therapeutics.

-	~~Authors:~~ Stevers, ~~L.M.~~, Leysen, S.~~F.R~~., ~~Ottmann, C~~.	+	Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR.,Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C Proc Natl Acad Sci U S A. 2016 Mar 1;113(9):E1152-61. doi:, 10.1073/pnas.1516631113. Epub 2016 Feb 17. PMID:26888287<ref>PMID:26888287</ref>

-	~~Description: Crystal structure~~ of ~~human 14~~-3-~~3 zeta in complex with CFTR R~~-~~domain peptide pS753~~-~~pS768~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5d2d" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Channel-conductance-controlling ATPase]]
		+	[[Category: Leysen, S F.R]]
	[[Category: Ottmann, C]]		[[Category: Ottmann, C]]
-	[[Category: Stevers, L.M]]	+	[[Category: Stevers, L M]]
-	[[Category: ~~Leysen, S.F.R~~]]	+	[[Category: Peptide binding protein]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Protein-peptide complex]]
		+	[[Category: Tandem binding]]

OCA: Protected "5d2d" [edit=sysop:move=sysop]

2015-08-12T13:44:42Z

Protected "5d2d" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:44, 12 August 2015

OCA: New page: '''Unreleased structure''' The entry 5d2d is ON HOLD Authors: Stevers, L.M., Leysen, S.F.R., Ottmann, C. Description: Crystal structure of human 14-3-3 zeta in complex with CFTR R-doma...

2015-08-12T13:44:41Z

New page: '''Unreleased structure''' The entry 5d2d is ON HOLD Authors: Stevers, L.M., Leysen, S.F.R., Ottmann, C. Description: Crystal structure of human 14-3-3 zeta in complex with CFTR R-doma...

New page

'''Unreleased structure'''

The entry 5d2d is ON HOLD

Authors: Stevers, L.M., Leysen, S.F.R., Ottmann, C.

Description: Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768
[[Category: Unreleased Structures]]
[[Category: Ottmann, C]]
[[Category: Stevers, L.M]]
[[Category: Leysen, S.F.R]]