1hhn - Revision history

OCA at 05:31, 15 May 2024

2024-05-15T05:31:19Z

←Older revision		Revision as of 05:31, 15 May 2024
Line 19:		Line 19:
	</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=1hhn 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=1hhn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The NMR structure of the rat calreticulin P-domain, comprising residues 189-288, CRT(189-288), shows a hairpin fold that involves the entire polypeptide chain, has the two chain ends in close spatial proximity, and does not fold back on itself. This globally extended structure is stabilized by three antiparallel beta-sheets, with the beta-strands comprising the residues 189-192 and 276-279, 206-209 and 262-265, and 223-226 and 248-251, respectively. The hairpin loop of residues 227-247 and the two connecting regions between the beta-sheets contain a hydrophobic cluster, where each of the three clusters includes two highly conserved tryptophyl residues, one from each strand of the hairpin. The three beta-sheets and the three hydrophobic clusters form a repeating pattern of interactions across the hairpin that reflects the periodicity of the amino acid sequence, which consists of three 17-residue repeats followed by three 14-residue repeats. Within the global hairpin fold there are two well-ordered subdomains comprising the residues 219-258, and 189-209 and 262-284, respectively. These are separated by a poorly ordered linker region, so that the relative orientation of the two subdomains cannot be precisely described. The structure type observed for CRT(189-288) provides an additional basis for functional studies of the abundant endoplasmic reticulum chaperone calreticulin.
		+
		+	NMR structure of the calreticulin P-domain.,Ellgaard L, Riek R, Herrmann T, Guntert P, Braun D, Helenius A, Wuthrich K Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3133-8. Epub 2001 Mar 6. PMID:11248044<ref>PMID:11248044</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1hhn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Calreticulin 3D structures\|Calreticulin 3D structures]]		*[[Calreticulin 3D structures\|Calreticulin 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:31, 27 March 2024

2024-03-27T11:31:59Z

←Older revision		Revision as of 11:31, 27 March 2024
Line 1:		Line 1:

	==Calreticulin P-domain==		==Calreticulin P-domain==
-	<StructureSection load='1hhn' size='340' side='right'caption='[[1hhn~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='1hhn' size='340' side='right'caption='[[1hhn]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HHN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HHN FirstGlance]. <br>
-	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [https://pdbe.org/1hhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [https://www.ebi.ac.uk/pdbsum/1hhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhn ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [https://pdbe.org/1hhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [https://www.ebi.ac.uk/pdbsum/1hhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CALR_RAT CALR_RAT]] 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).	+	[https://www.uniprot.org/uniprot/CALR_RAT CALR_RAT] 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).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 19:
	</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=1hhn 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=1hhn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The NMR structure of the rat calreticulin P-domain, comprising residues 189-288, CRT(189-288), shows a hairpin fold that involves the entire polypeptide chain, has the two chain ends in close spatial proximity, and does not fold back on itself. This globally extended structure is stabilized by three antiparallel beta-sheets, with the beta-strands comprising the residues 189-192 and 276-279, 206-209 and 262-265, and 223-226 and 248-251, respectively. The hairpin loop of residues 227-247 and the two connecting regions between the beta-sheets contain a hydrophobic cluster, where each of the three clusters includes two highly conserved tryptophyl residues, one from each strand of the hairpin. The three beta-sheets and the three hydrophobic clusters form a repeating pattern of interactions across the hairpin that reflects the periodicity of the amino acid sequence, which consists of three 17-residue repeats followed by three 14-residue repeats. Within the global hairpin fold there are two well-ordered subdomains comprising the residues 219-258, and 189-209 and 262-284, respectively. These are separated by a poorly ordered linker region, so that the relative orientation of the two subdomains cannot be precisely described. The structure type observed for CRT(189-288) provides an additional basis for functional studies of the abundant endoplasmic reticulum chaperone calreticulin.
-
-	NMR structure of the calreticulin P-domain.,Ellgaard L, Riek R, Herrmann T, Guntert P, Braun D, Helenius A, Wuthrich K Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3133-8. Epub 2001 Mar 6. PMID:11248044<ref>PMID:11248044</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1hhn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Calreticulin 3D structures\|Calreticulin 3D structures]]		*[[Calreticulin 3D structures\|Calreticulin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Braun, D]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Ellgaard, L]]	+	[[Category: Braun D]]
-	[[Category: Guntert, P]]	+	[[Category: Ellgaard L]]
-	[[Category: Helenius, A]]	+	[[Category: Guntert P]]
-	[[Category: Herrmann, T]]	+	[[Category: Helenius A]]
-	[[Category: Riek, R]]	+	[[Category: Herrmann T]]
-	[[Category: Wuthrich, K]]	+	[[Category: Riek R]]
-	~~[[Category: Molecular chaperone~~]]	+	[[Category: Wuthrich K]]

OCA at 10:49, 4 August 2021

2021-08-04T10:49:29Z

←Older revision		Revision as of 10:49, 4 August 2021
Line 3:		Line 3:
	<StructureSection load='1hhn' size='340' side='right'caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1hhn' size='340' side='right'caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1HHN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HHN FirstGlance]. <br>
-	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [~~http~~://pdbe.org/1hhn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1hhn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhn ProSAT]</span></td></tr>	+	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [https://pdbe.org/1hhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [https://www.ebi.ac.uk/pdbsum/1hhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CALR_RAT CALR_RAT]] 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).	+	[[https://www.uniprot.org/uniprot/CALR_RAT CALR_RAT]] 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).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:27, 30 October 2019

2019-10-30T10:27:39Z

←Older revision		Revision as of 10:27, 30 October 2019
Line 1:		Line 1:

	==Calreticulin P-domain==		==Calreticulin P-domain==
-	<StructureSection load='1hhn' size='340' side='right' caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='1hhn' size='340' side='right'caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>
Line 27:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1hhn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1hhn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Calreticulin 3D structures\|Calreticulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Braun, D]]		[[Category: Braun, D]]
	[[Category: Ellgaard, L]]		[[Category: Ellgaard, L]]

OCA at 09:28, 10 January 2018

2018-01-10T09:28:07Z

←Older revision		Revision as of 09:28, 10 January 2018
Line 1:		Line 1:
-	==~~CALRETICULIN~~ P-~~DOMAIN~~==	+
		+	==Calreticulin P-domain==
	<StructureSection load='1hhn' size='340' side='right' caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1hhn' size='340' side='right' caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>
-	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://pdbe.org/1hhn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn PDBsum]</span></td></tr>	+	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://pdbe.org/1hhn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/1hhn_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/1hhn_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 03:10, 8 February 2016

2016-02-08T03:10:07Z

←Older revision		Revision as of 03:10, 8 February 2016
Line 15:		Line 15:
	<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=1hhn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:18, 10 September 2015

2015-09-10T07:18:15Z

←Older revision		Revision as of 07:18, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1hhn' size='340' side='right' caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1hhn' size='340' side='right' caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>
-	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn PDBsum]</span></td></tr>	+	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://pdbe.org/1hhn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 25:
	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 1hhn" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Braun, D]]		[[Category: Braun, D]]
	[[Category: Ellgaard, L]]		[[Category: Ellgaard, L]]

OCA at 20:08, 24 December 2014

2014-12-24T20:08:46Z

←Older revision		Revision as of 20:08, 24 December 2014
Line 5:		Line 5:
	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn PDBsum]</span></td></tr>		</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CALR_RAT CALR_RAT]] 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).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:18, 22 December 2014

2014-12-22T22:18:59Z

←Older revision		Revision as of 22:18, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>
-	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn PDBsum]</span></td></tr>	+	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn 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 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Braun, D.]]	+	[[Category: Braun, D]]
-	[[Category: Ellgaard, L.]]	+	[[Category: Ellgaard, L]]
-	[[Category: Guntert, P.]]	+	[[Category: Guntert, P]]
-	[[Category: Helenius, A.]]	+	[[Category: Helenius, A]]
-	[[Category: Herrmann, T.]]	+	[[Category: Herrmann, T]]
-	[[Category: Riek, R.]]	+	[[Category: Riek, R]]
-	[[Category: Wuthrich, K.]]	+	[[Category: Wuthrich, K]]
	[[Category: Molecular chaperone]]		[[Category: Molecular chaperone]]

OCA at 16:10, 29 September 2014

2014-09-29T16:10:18Z

←Older revision		Revision as of 16:10, 29 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1hhn.~~png\|left~~\|200px]]	+	==CALRETICULIN P-DOMAIN==
		+	<StructureSection load='1hhn' size='340' side='right' caption='[[1hhn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1hhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHN FirstGlance]. <br>
		+	</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=1hhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hhn RCSB], [http://www.ebi.ac.uk/pdbsum/1hhn 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/hh/1hhn_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 NMR structure of the rat calreticulin P-domain, comprising residues 189-288, CRT(189-288), shows a hairpin fold that involves the entire polypeptide chain, has the two chain ends in close spatial proximity, and does not fold back on itself. This globally extended structure is stabilized by three antiparallel beta-sheets, with the beta-strands comprising the residues 189-192 and 276-279, 206-209 and 262-265, and 223-226 and 248-251, respectively. The hairpin loop of residues 227-247 and the two connecting regions between the beta-sheets contain a hydrophobic cluster, where each of the three clusters includes two highly conserved tryptophyl residues, one from each strand of the hairpin. The three beta-sheets and the three hydrophobic clusters form a repeating pattern of interactions across the hairpin that reflects the periodicity of the amino acid sequence, which consists of three 17-residue repeats followed by three 14-residue repeats. Within the global hairpin fold there are two well-ordered subdomains comprising the residues 219-258, and 189-209 and 262-284, respectively. These are separated by a poorly ordered linker region, so that the relative orientation of the two subdomains cannot be precisely described. The structure type observed for CRT(189-288) provides an additional basis for functional studies of the abundant endoplasmic reticulum chaperone calreticulin.

-	~~{{STRUCTURE_1hhn\| PDB=1hhn \| SCENE= }}~~	+	NMR structure of the calreticulin P-domain.,Ellgaard L, Riek R, Herrmann T, Guntert P, Braun D, Helenius A, Wuthrich K Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3133-8. Epub 2001 Mar 6. PMID:11248044<ref>PMID:11248044</ref>

-	~~===CALRETICULIN P-DOMAIN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11248044}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1hhn]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Rattus_norvegicus Rattus norvegicus]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1HHN OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:011248044<~~/~~ref~~><~~ref group="xtra">PMID:011163798</ref><references group="xtra"~~/>	+
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Braun, D.]]		[[Category: Braun, D.]]