4ju5 - Revision history

OCA at 15:49, 20 September 2023

OCA — Wed, 20 Sep 2023 15:49:00 GMT

←Older revision		Revision as of 15:49, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JU5 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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [https://pdbe.org/4ju5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ju5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ju5 ProSAT]</span></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]] 2.28Å</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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [https://pdbe.org/4ju5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ju5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ju5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 11:25, 30 November 2022

OCA — Wed, 30 Nov 2022 11:25:27 GMT

←Older revision		Revision as of 11:25, 30 November 2022
Line 3:		Line 3:
	<StructureSection load='4ju5' size='340' side='right'caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='4ju5' size='340' side='right'caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [https://pdbe.org/4ju5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ju5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ju5 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [~~http~~://pdbe.org/4ju5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ju5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ju5 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>	+	[https://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Protein disulfide-isomerase]]~~	+	[[Category: Bastos-Aristizabal S]]
-	[[Category: Bastos-Aristizabal, S]]	+	[[Category: Gehring K]]
-	[[Category: Gehring, K]]	+	[[Category: Kozlov G]]
-	[[Category: Kozlov, G]]	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Disulfide isomerase]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Thioredoxin-like fold~~]]	+

OCA at 12:02, 17 July 2019

OCA — Wed, 17 Jul 2019 12:02:23 GMT

←Older revision		Revision as of 12:02, 17 July 2019
Line 1:		Line 1:

	==Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase==		==Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase==
-	<StructureSection load='4ju5' size='340' side='right' caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>	+	<StructureSection load='4ju5' size='340' side='right'caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>
Line 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Protein disulfide-isomerase]]		[[Category: Protein disulfide-isomerase]]
	[[Category: Bastos-Aristizabal, S]]		[[Category: Bastos-Aristizabal, S]]

OCA at 18:43, 4 August 2016

OCA — Thu, 04 Aug 2016 18:43:13 GMT

←Older revision		Revision as of 18:43, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase==		==Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase==
	<StructureSection load='4ju5' size='340' side='right' caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='4ju5' size='340' side='right' caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([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/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ju5 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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [http://pdbe.org/4ju5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ju5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ju5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4ju5" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:03, 25 December 2014

OCA — Thu, 25 Dec 2014 12:03:30 GMT

←Older revision		Revision as of 12:03, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ju5 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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ju5 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 15:
	Structural insight into the dimerization of human protein disulfide isomerase.,Bastos-Aristizabal S, Kozlov G, Gehring K Protein Sci. 2014 Feb 18. doi: 10.1002/pro.2444. PMID:24549644<ref>PMID:24549644</ref>		Structural insight into the dimerization of human protein disulfide isomerase.,Bastos-Aristizabal S, Kozlov G, Gehring K Protein Sci. 2014 Feb 18. doi: 10.1002/pro.2444. PMID:24549644<ref>PMID:24549644</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 21:		Line 23:
	[[Category: Human]]		[[Category: Human]]
	[[Category: Protein disulfide-isomerase]]		[[Category: Protein disulfide-isomerase]]
-	[[Category: Bastos-Aristizabal, S.]]	+	[[Category: Bastos-Aristizabal, S]]
-	[[Category: Gehring, K.]]	+	[[Category: Gehring, K]]
-	[[Category: Kozlov, G.]]	+	[[Category: Kozlov, G]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Disulfide isomerase]]		[[Category: Disulfide isomerase]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Thioredoxin-like fold]]		[[Category: Thioredoxin-like fold]]

OCA at 13:30, 18 May 2014

OCA — Sun, 18 May 2014 13:30:31 GMT

←Older revision		Revision as of 13:30, 18 May 2014
Line 2:		Line 2:
	<StructureSection load='4ju5' size='340' side='right' caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='4ju5' size='340' side='right' caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. <br>	+	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JU5 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.~~2 2~~.7.1.2] </span></td></tr>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ju5 PDBsum]</span></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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ju5 PDBsum]</span></td></tr>
	<table>		<table>

OCA at 07:03, 7 May 2014

OCA — Wed, 07 May 2014 07:03:06 GMT

←Older revision		Revision as of 07:03, 7 May 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ju5\| PDB=4ju5 \| SCENE= }}~~	+	==Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase==
-	===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase===	+	<StructureSection load='4ju5' size='340' side='right' caption='[[4ju5]], [[Resolution\|resolution]] 2.28Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24549644}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ju5]] 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=4JU5 OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HB, ERBA2L, PDI, PDIA1, PO4DB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=4ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ju5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ju5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ju5 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein disulfide isomerases (PDIs) are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum (ER). Here, it is shown that human PDI (PDIA1) dimerizes in vivo and proposed that the dimerization of PDI has physiological relevance by autoregulating its activity. The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 A resolution revealed that the formation of dimers occludes the substrate binding site and may function as a mechanism to regulate PDI activity in the ER.

-	~~==Function==~~	+	Structural insight into the dimerization of human protein disulfide isomerase.,Bastos-Aristizabal S, Kozlov G, Gehring K Protein Sci. 2014 Feb 18. doi: 10.1002/pro.2444. PMID:24549644<ref>PMID:24549644</ref>
-	~~[[http://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes~~ the ~~formation, breakage and rearrangement~~ of disulfide ~~bonds~~. ~~At the cell surface~~, ~~seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell~~, ~~seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations~~, ~~functions as a chaperone that inhibits aggregation of misfolded proteins~~. ~~At low concentrations, facilitates aggregation (anti-chaperone activity)~~. ~~May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis~~. ~~Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP~~.~~<ref>~~PMID:~~10636893</ref>~~ <ref>PMID:~~12485997~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4ju5]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4JU5 OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024549644</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Protein disulfide-isomerase]]		[[Category: Protein disulfide-isomerase]]
	[[Category: Bastos-Aristizabal, S.]]		[[Category: Bastos-Aristizabal, S.]]

OCA at 09:12, 19 March 2014

OCA — Wed, 19 Mar 2014 09:12:09 GMT

←Older revision		Revision as of 09:12, 19 March 2014
Line 1:		Line 1:
	{{STRUCTURE_4ju5\| PDB=4ju5 \| SCENE= }}		{{STRUCTURE_4ju5\| PDB=4ju5 \| SCENE= }}
	===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase===		===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase===
		+	{{ABSTRACT_PUBMED_24549644}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024549644</ref><references group="xtra"/><references/>
	[[Category: Protein disulfide-isomerase]]		[[Category: Protein disulfide-isomerase]]
	[[Category: Bastos-Aristizabal, S.]]		[[Category: Bastos-Aristizabal, S.]]

OCA at 17:47, 19 February 2014

OCA — Wed, 19 Feb 2014 17:47:54 GMT

←Older revision		Revision as of 17:47, 19 February 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure'''	+	{{STRUCTURE_4ju5\| PDB=4ju5 \| SCENE= }}
		+	===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase===

-	~~The entry 4ju5 is ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>

-	~~Authors~~: ~~Bastos-Aristizabal, S~~.~~, Kozlov, G~~.~~, Gehring, K~~.	+	==About this Structure==
		+	[[4ju5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JU5 OCA].

-	~~Description~~: ~~Crystal structure of the dimeric form of the bb' domains of human protein~~ disulfide isomerase	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Protein disulfide-isomerase]]
		+	[[Category: Bastos-Aristizabal, S.]]
		+	[[Category: Gehring, K.]]
		+	[[Category: Kozlov, G.]]
		+	[[Category: Chaperone]]
		+	[[Category: Disulfide isomerase]]
		+	[[Category: Isomerase]]
		+	[[Category: Thioredoxin-like fold]]

OCA at 10:55, 24 April 2013

OCA — Wed, 24 Apr 2013 10:55:45 GMT

←Older revision		Revision as of 10:55, 24 April 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ju5 is ON HOLD	+	The entry 4ju5 is ON HOLD until Paper Publication

	Authors: Bastos-Aristizabal, S., Kozlov, G., Gehring, K.		Authors: Bastos-Aristizabal, S., Kozlov, G., Gehring, K.

	Description: Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase		Description: Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase