1wyx - Revision history

OCA at 13:35, 13 March 2024

OCA — Wed, 13 Mar 2024 13:35:20 GMT

←Older revision		Revision as of 13:35, 13 March 2024
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	<StructureSection load='1wyx' size='340' side='right'caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>		<StructureSection load='1wyx' size='340' side='right'caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.14Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [https://pdbe.org/1wyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [https://www.ebi.ac.uk/pdbsum/1wyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wyx 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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [https://pdbe.org/1wyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [https://www.ebi.ac.uk/pdbsum/1wyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wyx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN]] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</ref>	+	[https://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</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=1wyx 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=1wyx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The Crk-associated tyrosine kinase substrate p130cas (CAS) is a docking protein containing an SH3 domain near its N terminus, followed by a short proline-rich segment, a large central substrate domain composed of 15 repeats of the four amino acid sequence YxxP, a serine-rich region and a carboxy-terminal domain, which possesses consensus binding sites for the SH2 and SH3 domains of Src (YDYV and RPLPSPP, respectively). The SH3 domain of CAS mediates its interaction with several proteins involved in signaling pathways such as focal adhesion kinase (FAK), tyrosine phosphatases PTP1B and PTP-PEST, and the guanine nucleotide exchange factor C3G. As a homolog of the corresponding Src docking domain, the CAS SH3 domain binds to proline-rich sequences (PxxP) of its interacting partners that can adopt a polyproline type II helix. We have determined a high-resolution X-ray structure of the recombinant human CAS SH3 domain. The domain, residues 1-69, crystallized in two related space groups, P2(1) and C222(1), that provided diffraction data to 1.1 A and 2.1 A, respectively. The crystal structure shows, in addition to the conserved SH3 domain architecture, the way in which the CAS characteristic amino acids form an atypically charged ligand-binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by the CAS SH3 domain. The structure enables modelling of the docking interactions to its ligands, for example from focal adhesion kinase, and supports structure-based drug design of inhibitors of the CAS-FAK interaction.
-
-	The 1.1 A resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity.,Wisniewska M, Bossenmaier B, Georges G, Hesse F, Dangl M, Kunkele KP, Ioannidis I, Huber R, Engh RA J Mol Biol. 2005 Apr 15;347(5):1005-14. PMID:15784259<ref>PMID:15784259</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1wyx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bossenmaier, B]]	+	[[Category: Bossenmaier B]]
-	[[Category: Dangl, M]]	+	[[Category: Dangl M]]
-	[[Category: Engh~~, R A~~]]	+	[[Category: Engh RA]]
-	[[Category: Georges, G]]	+	[[Category: Georges G]]
-	[[Category: Hesse, F]]	+	[[Category: Hesse F]]
-	[[Category: Huber, R]]	+	[[Category: Huber R]]
-	[[Category: Ioannidis, I]]	+	[[Category: Ioannidis I]]
-	[[Category: Kuenkele~~, K P~~]]	+	[[Category: Kuenkele KP]]
-	[[Category: Wisniewska, M]]	+	[[Category: Wisniewska M]]
-	~~[[Category: Beta sheet]]~~	+
-	~~[[Category: Cell adhesion~~]]	+

OCA at 16:30, 27 October 2021

OCA — Wed, 27 Oct 2021 16:30:32 GMT

←Older revision		Revision as of 16:30, 27 October 2021
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	<StructureSection load='1wyx' size='340' side='right'caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>		<StructureSection load='1wyx' size='340' side='right'caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1WYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [~~http~~://pdbe.org/1wyx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1wyx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1wyx 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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [https://pdbe.org/1wyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [https://www.ebi.ac.uk/pdbsum/1wyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wyx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN]] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</ref>	+	[[https://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN]] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 17:13, 22 January 2020

OCA — Wed, 22 Jan 2020 17:13:56 GMT

←Older revision		Revision as of 17:13, 22 January 2020
Line 1:		Line 1:

	==The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution==		==The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution==
-	<StructureSection load='1wyx' size='340' side='right' caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>	+	<StructureSection load='1wyx' size='340' side='right'caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bossenmaier, B]]		[[Category: Bossenmaier, B]]
	[[Category: Dangl, M]]		[[Category: Dangl, M]]

OCA at 16:00, 11 April 2018

OCA — Wed, 11 Apr 2018 16:00:09 GMT

←Older revision		Revision as of 16:00, 11 April 2018
Line 1:		Line 1:
		+
	==The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution==		==The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution==
	<StructureSection load='1wyx' size='340' side='right' caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>		<StructureSection load='1wyx' size='340' side='right' caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [http://pdbe.org/1wyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [http://www.ebi.ac.uk/pdbsum/1wyx 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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [http://pdbe.org/1wyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [http://www.ebi.ac.uk/pdbsum/1wyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wyx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wy/1wyx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wy/1wyx_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 16:01, 8 February 2016

OCA — Mon, 08 Feb 2016 16:01:48 GMT

←Older revision		Revision as of 16:01, 8 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=1wyx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 13:11, 10 September 2015

OCA — Thu, 10 Sep 2015 13:11:51 GMT

←Older revision		Revision as of 13:11, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1wyx' size='340' side='right' caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>		<StructureSection load='1wyx' size='340' side='right' caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [http://www.ebi.ac.uk/pdbsum/1wyx 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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [http://pdbe.org/1wyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [http://www.ebi.ac.uk/pdbsum/1wyx PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN]] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		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 1wyx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bossenmaier, B]]		[[Category: Bossenmaier, B]]
	[[Category: Dangl, M]]		[[Category: Dangl, M]]

OCA at 12:17, 6 January 2015

OCA — Tue, 06 Jan 2015 12:17:59 GMT

←Older revision		Revision as of 12:17, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [http://www.ebi.ac.uk/pdbsum/1wyx 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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [http://www.ebi.ac.uk/pdbsum/1wyx 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 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bossenmaier, B.]]	+	[[Category: Bossenmaier, B]]
-	[[Category: Dangl, M.]]	+	[[Category: Dangl, M]]
-	[[Category: Engh, R A.]]	+	[[Category: Engh, R A]]
-	[[Category: Georges, G.]]	+	[[Category: Georges, G]]
-	[[Category: Hesse, F.]]	+	[[Category: Hesse, F]]
-	[[Category: Huber, R.]]	+	[[Category: Huber, R]]
-	[[Category: Ioannidis, I.]]	+	[[Category: Ioannidis, I]]
-	[[Category: Kuenkele, K P.]]	+	[[Category: Kuenkele, K P]]
-	[[Category: Wisniewska, M.]]	+	[[Category: Wisniewska, M]]
	[[Category: Beta sheet]]		[[Category: Beta sheet]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]

OCA at 20:18, 29 September 2014

OCA — Mon, 29 Sep 2014 20:18:22 GMT

←Older revision		Revision as of 20:18, 29 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1wyx.~~png\|left~~\|200px]]	+	==The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution==
		+	<StructureSection load='1wyx' size='340' side='right' caption='[[1wyx]], [[Resolution\|resolution]] 1.14Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1wyx]] 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=1WYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WYX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<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=1wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wyx RCSB], [http://www.ebi.ac.uk/pdbsum/1wyx 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/wy/1wyx_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 ==
		+	The Crk-associated tyrosine kinase substrate p130cas (CAS) is a docking protein containing an SH3 domain near its N terminus, followed by a short proline-rich segment, a large central substrate domain composed of 15 repeats of the four amino acid sequence YxxP, a serine-rich region and a carboxy-terminal domain, which possesses consensus binding sites for the SH2 and SH3 domains of Src (YDYV and RPLPSPP, respectively). The SH3 domain of CAS mediates its interaction with several proteins involved in signaling pathways such as focal adhesion kinase (FAK), tyrosine phosphatases PTP1B and PTP-PEST, and the guanine nucleotide exchange factor C3G. As a homolog of the corresponding Src docking domain, the CAS SH3 domain binds to proline-rich sequences (PxxP) of its interacting partners that can adopt a polyproline type II helix. We have determined a high-resolution X-ray structure of the recombinant human CAS SH3 domain. The domain, residues 1-69, crystallized in two related space groups, P2(1) and C222(1), that provided diffraction data to 1.1 A and 2.1 A, respectively. The crystal structure shows, in addition to the conserved SH3 domain architecture, the way in which the CAS characteristic amino acids form an atypically charged ligand-binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by the CAS SH3 domain. The structure enables modelling of the docking interactions to its ligands, for example from focal adhesion kinase, and supports structure-based drug design of inhibitors of the CAS-FAK interaction.

-	~~{{STRUCTURE_1wyx\| PDB=1wyx \| SCENE= }}~~	+	The 1.1 A resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity.,Wisniewska M, Bossenmaier B, Georges G, Hesse F, Dangl M, Kunkele KP, Ioannidis I, Huber R, Engh RA J Mol Biol. 2005 Apr 15;347(5):1005-14. PMID:15784259<ref>PMID:15784259</ref>

-	~~===The Crystal Structure~~ of the ~~p130Cas SH3 Domain at 1~~.~~1 A Resolution===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15784259}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1wyx]] 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=1WYX OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015784259<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bossenmaier, B.]]		[[Category: Bossenmaier, B.]]

OCA: Protected "1wyx" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 10:56:24 GMT

Protected "1wyx" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:56, 5 January 2013

OCA at 10:56, 5 January 2013

OCA — Sat, 05 Jan 2013 10:56:22 GMT

←Older revision		Revision as of 10:56, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1wyx.png\|left\|200px]]		[[Image:1wyx.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1wyx", 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_1wyx\| PDB=1wyx \| SCENE= }}		{{STRUCTURE_1wyx\| PDB=1wyx \| SCENE= }}

	===The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution===		===The Crystal Structure of the p130Cas SH3 Domain at 1.1 A Resolution===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15784259}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15784259 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15784259}}		{{ABSTRACT_PUBMED_15784259}}

	==About this Structure==		==About this Structure==
-	~~1WYX~~ is a 2 ~~chains~~ structure ~~of sequences~~ 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=1WYX OCA].	+	[[1wyx]] 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=1WYX OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15784259~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015784259</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bossenmaier, B.]]		[[Category: Bossenmaier, B.]]
Line 35:		Line 23:
	[[Category: Wisniewska, M.]]		[[Category: Wisniewska, M.]]
	[[Category: Beta sheet]]		[[Category: Beta sheet]]
-		+	[[Category: Cell adhesion]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 00:17:14 2009''~~	+