3o0v - Revision history

OCA at 09:25, 6 September 2023

OCA — Wed, 06 Sep 2023 09:25:22 GMT

←Older revision		Revision as of 09:25, 6 September 2023
Line 1:		Line 1:

	==Crystal structure of the calreticulin lectin domain==		==Crystal structure of the calreticulin lectin domain==
-	<StructureSection load='3o0v' size='340' side='right' caption='[[3o0v]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3o0v' size='340' side='right'caption='[[3o0v]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3o0v]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3O0V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3o0v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O0V FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.3Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o0w\|3o0w]]~~, [[~~3o0x~~\|~~3o0x~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~Calr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=10090 LK3 transgenic mice])~~</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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [https://pdbe.org/3o0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [https://www.ebi.ac.uk/pdbsum/3o0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0v ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [~~http~~://pdbe.org/3o0v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3o0v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0v ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CALR_MOUSE CALR_MOUSE]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:20880849</ref> <ref>PMID:21652723</ref>	+	[https://www.uniprot.org/uniprot/CALR_MOUSE CALR_MOUSE] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:20880849</ref> <ref>PMID:21652723</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/3o0v_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/3o0v_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>
Line 30:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 3o0v" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3o0v" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calreticulin 3D structures\|Calreticulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Gehring, K~~]]	+	[[Category: Mus musculus]]
-	[[Category: ~~Kozlov, G~~]]	+	[[Category: Gehring K]]
-	[[Category: ~~Calcium binding]]~~	+	[[Category: Kozlov G]]
-	~~[[Category: Carbohydrate binding]]~~	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Jelly roll fold~~]]	+

OCA at 18:37, 4 August 2016

OCA — Thu, 04 Aug 2016 18:37:52 GMT

←Older revision		Revision as of 18:37, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the calreticulin lectin domain==		==Crystal structure of the calreticulin lectin domain==
	<StructureSection load='3o0v' size='340' side='right' caption='[[3o0v]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3o0v' size='340' side='right' caption='[[3o0v]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3o0v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O0V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3o0v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O0V FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o0w\|3o0w]], [[3o0x\|3o0x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o0w\|3o0w]], [[3o0x\|3o0x]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [http://www.ebi.ac.uk/pdbsum/3o0v 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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [http://pdbe.org/3o0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [http://www.ebi.ac.uk/pdbsum/3o0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0v ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~Q3TVD2_MOUSE Q3TVD2_MOUSE~~]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:20880849</ref> <ref>PMID:21652723</ref>	+	[[http://www.uniprot.org/uniprot/CALR_MOUSE CALR_MOUSE]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:20880849</ref> <ref>PMID:21652723</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 19:
	<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=3o0v ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	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 3o0v" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Gehring, K]]		[[Category: Gehring, K]]
	[[Category: Kozlov, G]]		[[Category: Kozlov, G]]

OCA at 11:58, 25 December 2014

OCA — Thu, 25 Dec 2014 11:58:58 GMT

←Older revision		Revision as of 11:58, 25 December 2014
Line 8:		Line 8:
	<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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [http://www.ebi.ac.uk/pdbsum/3o0v 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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [http://www.ebi.ac.uk/pdbsum/3o0v PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q3TVD2_MOUSE Q3TVD2_MOUSE]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:20880849</ref> <ref>PMID:21652723</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:06, 19 December 2014

OCA — Fri, 19 Dec 2014 07:06:32 GMT

←Older revision		Revision as of 07:06, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3o0v~~\| ~~PDB~~=3o0v \| ~~SCENE~~= }}	+	==Crystal structure of the calreticulin lectin domain==
-	===~~Crystal~~ structure of the ~~calreticulin lectin domain~~===	+	<StructureSection load='3o0v' size='340' side='right' caption='[[3o0v]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20880849}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3o0v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O0V FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o0w\|3o0w]], [[3o0x\|3o0x]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Calr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [http://www.ebi.ac.uk/pdbsum/3o0v 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/o0/3o0v_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 calnexin cycle is a process by which glycosylated proteins are subjected to folding cycles in the endoplasmic reticulum lumen via binding to the membrane protein calnexin (CNX) or to its soluble homolog calreticulin (CRT). CNX and CRT specifically recognize monoglucosylated Glc(1)Man(9)GlcNAc(2) glycans, but the structural determinants underlying this specificity are unknown. Here, we report a 1.95-A crystal structure of the CRT lectin domain in complex with the tetrasaccharide alpha-Glc-(1-->3)-alpha-Man-(1-->2)-alpha-Man-(1-->2)-Man. The tetrasaccharide binds to a long channel on CRT formed by a concave beta-sheet. All four sugar moieties are engaged in the protein binding via an extensive network of hydrogen bonds and hydrophobic contacts. The structure explains the requirement for glucose at the nonreducing end of the carbohydrate; the oxygen O(2) of glucose perfectly fits to a pocket formed by CRT side chains while forming direct hydrogen bonds with the carbonyl of Gly(124) and the side chain of Lys(111). The structure also explains a requirement for the Cys(105)-Cys(137) disulfide bond in CRT/CNX for efficient carbohydrate binding. The Cys(105)-Cys(137) disulfide bond is involved in intimate contacts with the third and fourth sugar moieties of the Glc(1)Man(3) tetrasaccharide. Finally, the structure rationalizes previous mutagenesis of CRT and lays a structural groundwork for future studies of the role of CNX/CRT in diverse biological pathways.

-	~~==Function==~~	+	Structural basis of carbohydrate recognition by calreticulin.,Kozlov G, Pocanschi CL, Rosenauer A, Bastos-Aristizabal S, Gorelik A, Williams DB, Gehring K J Biol Chem. 2010 Dec 3;285(49):38612-20. Epub 2010 Sep 29. PMID:20880849<ref>PMID:20880849</ref>
-	~~[[http://www~~.~~uniprot.org/uniprot/Q3TVD2_MOUSE Q3TVD2_MOUSE]] Calcium~~-~~binding chaperone that promotes folding~~, ~~oligomeric assembly and quality control in the endoplasmic reticulum~~ (ER) ~~via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA~~-~~binding domain of NR3C1 and mediates its nuclear export~~. ~~Involved in maternal gene expression regulation~~. ~~May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>~~PMID:20880849~~</ref>~~ <ref>PMID:~~21652723~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3o0v]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Mus_musculus Mus musculus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020880849</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Gehring, K.]]	+	[[Category: Gehring, K]]
-	[[Category: Kozlov, G.]]	+	[[Category: Kozlov, G]]
	[[Category: Calcium binding]]		[[Category: Calcium binding]]
	[[Category: Carbohydrate binding]]		[[Category: Carbohydrate binding]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Jelly roll fold]]		[[Category: Jelly roll fold]]

OCA: Protected "3o0v" [edit=sysop:move=sysop]

OCA — Wed, 24 Apr 2013 11:47:59 GMT

Protected "3o0v" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:47, 24 April 2013

OCA at 11:47, 24 April 2013

OCA — Wed, 24 Apr 2013 11:47:57 GMT

←Older revision		Revision as of 11:47, 24 April 2013
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-	{{Seed}}
-	[[Image:3o0v.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3o0v", 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_3o0v\| PDB=3o0v \| SCENE= }}		{{STRUCTURE_3o0v\| PDB=3o0v \| SCENE= }}
-
	===Crystal structure of the calreticulin lectin domain===		===Crystal structure of the calreticulin lectin domain===
		+	{{ABSTRACT_PUBMED_20880849}}

-		+	==Function==
-	~~<!--~~	+	[[http://www.uniprot.org/uniprot/Q3TVD2_MOUSE Q3TVD2_MOUSE]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:20880849</ref> <ref>PMID:21652723</ref>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_20880849}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 20880849 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20880849}}~~	+

	==About this Structure==		==About this Structure==
-	~~3O0V~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA].	+	[[3o0v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20880849~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020880849</ref><references group="xtra"/><references/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Gehring, K.]]		[[Category: Gehring, K.]]
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	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Jelly roll fold]]		[[Category: Jelly roll fold]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:22:18 2010''

OCA at 06:09, 22 December 2010

OCA — Wed, 22 Dec 2010 06:09:41 GMT

←Older revision		Revision as of 06:09, 22 December 2010
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	{{Seed}}		{{Seed}}
-	[[Image:3o0v.~~jpg~~\|left\|200px]]	+	[[Image:3o0v.png\|left\|200px]]

	<!--		<!--
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	===Crystal structure of the calreticulin lectin domain===		===Crystal structure of the calreticulin lectin domain===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20880849}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20880849 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20880849}}

	==About this Structure==		==About this Structure==
	3O0V is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA].		3O0V is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20880849</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Gehring, K.]]		[[Category: Gehring, K.]]
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	[[Category: Jelly roll fold]]		[[Category: Jelly roll fold]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Sep 29 08~~:16:07 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:22:18 2010''

OCA at 05:06, 29 September 2010

OCA — Wed, 29 Sep 2010 05:06:53 GMT

←Older revision		Revision as of 05:06, 29 September 2010
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-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3o0v.jpg\|left\|200px]]

-	The ~~entry 3o0v~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3o0v", 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_3o0v\| PDB=3o0v \| SCENE= }}

-	~~Authors: Kozlov, G., Gehring, K.~~	+	===Crystal structure of the calreticulin lectin domain===

-	Description: Crystal structure of the calreticulin lectin domain

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jul 28 12~~:27:29 2010''	+	==About this Structure==
		+	3O0V is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0V OCA].
		+	[[Category: Mus musculus]]
		+	[[Category: Gehring, K.]]
		+	[[Category: Kozlov, G.]]
		+	[[Category: Calcium binding]]
		+	[[Category: Carbohydrate binding]]
		+	[[Category: Chaperone]]
		+	[[Category: Jelly roll fold]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 29 08:16:07 2010''

OCA: New page: '''Unreleased structure''' The entry 3o0v is ON HOLD until Paper Publication Authors: Kozlov, G., Gehring, K. Description: Crystal structure of the calreticulin lectin domain ''Page s...

OCA — Wed, 28 Jul 2010 08:20:46 GMT

New page: '''Unreleased structure''' The entry 3o0v is ON HOLD until Paper Publication Authors: Kozlov, G., Gehring, K. Description: Crystal structure of the calreticulin lectin domain ''Page s...

New page

'''Unreleased structure'''

The entry 3o0v is ON HOLD until Paper Publication

Authors: Kozlov, G., Gehring, K.

Description: Crystal structure of the calreticulin lectin domain

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:27:29 2010''