3wht - Revision history

OCA at 13:11, 8 November 2023

OCA — Wed, 08 Nov 2023 13:11:14 GMT

←Older revision		Revision as of 13:11, 8 November 2023
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	<StructureSection load='3wht' size='340' side='right'caption='[[3wht]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3wht' size='340' side='right'caption='[[3wht]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wht]] 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=3WHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WHT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wht]] 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=3WHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WHT FirstGlance]. <br>
-	</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>~~, ~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.8Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3a4u\|3a4u]], [[1gv9\|1gv9]], [[1r1z\|1r1z]], [[4gky\|4gky]], [[4gkx\|4gkx]], [[3lcp\|3lcp]], [[3whu\|3whu]]~~</~~div~~><~~/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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<~~tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td><td class="sblockDat">ERGIC53 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MCFD2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wht OCA], [https://pdbe.org/3wht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wht RCSB], [https://www.ebi.ac.uk/pdbsum/3wht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wht 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=3wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wht OCA], [https://pdbe.org/3wht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wht RCSB], [https://www.ebi.ac.uk/pdbsum/3wht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wht ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[https://omim.org/entry/227300 227300]]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref> [[https://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:[https://omim.org/entry/613625 613625]]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:12717434</ref> <ref>PMID:18590741</ref>	+	[https://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[https://omim.org/entry/227300 227300]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref> <ref>PMID:12717434</ref> [[https://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.<ref>PMID:12717434</ref>	+	[https://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref> <ref>PMID:12717434</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kato, K]]	+	[[Category: Kato K]]
-	[[Category: Satoh, T]]	+	[[Category: Satoh T]]
-	[[Category: Suzuki, K]]	+	[[Category: Suzuki K]]
-	~~[[Category: Beta-sandwich]]~~	+
-	~~[[Category: Calcium binding]]~~	+
-	~~[[Category: Cargo receptor]]~~	+
-	~~[[Category: Ef-hand]]~~	+
-	~~[[Category: Er]]~~	+
-	~~[[Category: Ergic]]~~	+
-	~~[[Category: Protein transport~~]]	+

OCA at 05:37, 3 August 2022

OCA — Wed, 03 Aug 2022 05:37:08 GMT

←Older revision		Revision as of 05:37, 3 August 2022
Line 1:		Line 1:

	==Crystal structure of ERGIC-53/MCFD2, Calcium-free form==		==Crystal structure of ERGIC-53/MCFD2, Calcium-free form==
-	<StructureSection load='3wht' size='340' side='right' caption='[[3wht]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='3wht' size='340' side='right'caption='[[3wht]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wht]] 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=3WHT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3WHT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wht]] 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=3WHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WHT 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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a4u\|3a4u]], [[1gv9\|1gv9]], [[1r1z\|1r1z]], [[4gky\|4gky]], [[4gkx\|4gkx]], [[3lcp\|3lcp]], [[3whu\|3whu]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a4u\|3a4u]], [[1gv9\|1gv9]], [[1r1z\|1r1z]], [[4gky\|4gky]], [[4gkx\|4gkx]], [[3lcp\|3lcp]], [[3whu\|3whu]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERGIC53 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MCFD2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERGIC53 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MCFD2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wht OCA], [~~http~~://pdbe.org/3wht PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3wht RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3wht PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3wht 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=3wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wht OCA], [https://pdbe.org/3wht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wht RCSB], [https://www.ebi.ac.uk/pdbsum/3wht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wht ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[~~http~~://omim.org/entry/227300 227300]]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref> [[~~http~~://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:[~~http~~://omim.org/entry/613625 613625]]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:12717434</ref> <ref>PMID:18590741</ref>	+	[[https://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[https://omim.org/entry/227300 227300]]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref> [[https://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:[https://omim.org/entry/613625 613625]]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:12717434</ref> <ref>PMID:18590741</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref> <ref>PMID:12717434</ref> [[~~http~~://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.<ref>PMID:12717434</ref>	+	[[https://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref> <ref>PMID:12717434</ref> [[https://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.<ref>PMID:12717434</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 3wht" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3wht" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ERGIC-53\|ERGIC-53]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Kato, K]]		[[Category: Kato, K]]
	[[Category: Satoh, T]]		[[Category: Satoh, T]]

OCA at 10:01, 5 August 2016

OCA — Fri, 05 Aug 2016 10:01:51 GMT

←Older revision		Revision as of 10:01, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of ERGIC-53/MCFD2, Calcium-free form==		==Crystal structure of ERGIC-53/MCFD2, Calcium-free form==
	<StructureSection load='3wht' size='340' side='right' caption='[[3wht]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3wht' size='340' side='right' caption='[[3wht]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a4u\|3a4u]], [[1gv9\|1gv9]], [[1r1z\|1r1z]], [[4gky\|4gky]], [[4gkx\|4gkx]], [[3lcp\|3lcp]], [[3whu\|3whu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a4u\|3a4u]], [[1gv9\|1gv9]], [[1r1z\|1r1z]], [[4gky\|4gky]], [[4gkx\|4gkx]], [[3lcp\|3lcp]], [[3whu\|3whu]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERGIC53 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MCFD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERGIC53 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MCFD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wht RCSB], [http://www.ebi.ac.uk/pdbsum/3wht 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=3wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wht OCA], [http://pdbe.org/3wht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wht RCSB], [http://www.ebi.ac.uk/pdbsum/3wht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wht ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 3wht" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:34, 21 December 2014

OCA — Sun, 21 Dec 2014 18:34:22 GMT

←Older revision		Revision as of 18:34, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3wht\| PDB=3wht \| SCENE= }}~~	+	==Crystal structure of ERGIC-53/MCFD2, Calcium-free form==
-	===Crystal structure of ERGIC-53/MCFD2, Calcium-free form===	+	<StructureSection load='3wht' size='340' side='right' caption='[[3wht]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24498414}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3wht]] 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=3WHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WHT FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3a4u\|3a4u]], [[1gv9\|1gv9]], [[1r1z\|1r1z]], [[4gky\|4gky]], [[4gkx\|4gkx]], [[3lcp\|3lcp]], [[3whu\|3whu]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERGIC53 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MCFD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wht RCSB], [http://www.ebi.ac.uk/pdbsum/3wht PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[http://omim.org/entry/227300 227300]]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:[http://omim.org/entry/613625 613625]]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:12717434</ref> <ref>PMID:18590741</ref>		[[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[http://omim.org/entry/227300 227300]]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:[http://omim.org/entry/613625 613625]]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:12717434</ref> <ref>PMID:18590741</ref>
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref> <ref>PMID:12717434</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.<ref>PMID:12717434</ref>		[[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref> <ref>PMID:12717434</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.<ref>PMID:12717434</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	ERGIC-53 and VIP36 are categorized as leguminous type (L-type) lectins, and they function as cargo receptors for trafficking certain N-linked glycoproteins in the secretory pathway in animal cells. They share structural similarities in their carbohydrate recognition domains (CRDs) but exhibit distinct sugar-binding specificities and affinities. VIP36 specifically interacts with the alpha1,2-linked D1 mannosyl arm without terminal glucosylation, while ERGIC-53 shows a broader specificity and lower binding affinity to the high-mannose-type oligosaccharides, irrespective of the presence or absence of the non-reducing terminal glucose residue at the D1 arm. In this study, we determined the crystal structure of ERGIC-53-CRD in complex with their binding partner, MCFD2 and the alpha1,2 mannotriose which corresponds to the trisaccharide of the D1 arm of high-mannose-type glycans. ERGIC-53 can interact with the D1 trimannosyl arm in two alternative modes, one of which is similar but distinct from that previously observed for VIP36. ERGIC-53 has a shallower sugar-binding pocket than VIP36 because of the single amino acid substitution, Asp-to-Gly. This enables ERGIC-53 to accommodate the non-reducing terminal glucose of the D1 arm in its CRD. In the other interaction mode, the 3-OH group of the terminal mannose was situated outward with respect to the sugar binding pocket, also enabling the Glcalpha1-3 linkage formation without steric hindrance. Our findings thus provide a structural basis for the broad sugar-binding specificity of the ERGIC-53/MCFD2 cargo receptor complex.

-	~~==About this Structure==~~	+	Structural Basis for Disparate Sugar-Binding Specificities in the Homologous Cargo Receptors ERGIC-53 and VIP36.,Satoh T, Suzuki K, Yamaguchi T, Kato K PLoS One. 2014 Feb 3;9(2):e87963. doi: 10.1371/journal.pone.0087963. eCollection , 2014. PMID:24498414<ref>PMID:24498414</ref>
-	~~[[3wht]] is a~~ 2 ~~chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.~~il/oca-bin/ocashort?id=3WHT OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024498414</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Kato, K.]]	+	== References ==
-	[[Category: Satoh, T.]]	+	<references/>
-	[[Category: Suzuki, K.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Kato, K]]
		+	[[Category: Satoh, T]]
		+	[[Category: Suzuki, K]]
	[[Category: Beta-sandwich]]		[[Category: Beta-sandwich]]
	[[Category: Calcium binding]]		[[Category: Calcium binding]]

OCA at 14:30, 19 February 2014

OCA — Wed, 19 Feb 2014 14:30:21 GMT

←Older revision		Revision as of 14:30, 19 February 2014
Line 1:		Line 1:
	{{STRUCTURE_3wht\| PDB=3wht \| SCENE= }}		{{STRUCTURE_3wht\| PDB=3wht \| SCENE= }}
	===Crystal structure of ERGIC-53/MCFD2, Calcium-free form===		===Crystal structure of ERGIC-53/MCFD2, Calcium-free form===
		+	{{ABSTRACT_PUBMED_24498414}}

	==Disease==		==Disease==
Line 12:		Line 13:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024498414</ref><references group="xtra"/><references/>
	[[Category: Kato, K.]]		[[Category: Kato, K.]]
	[[Category: Satoh, T.]]		[[Category: Satoh, T.]]

OCA at 08:19, 15 January 2014

OCA — Wed, 15 Jan 2014 08:19:23 GMT

←Older revision		Revision as of 08:19, 15 January 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3wht\| PDB=3wht \| SCENE= }}
		+	===Crystal structure of ERGIC-53/MCFD2, Calcium-free form===

-	The entry ~~3wht~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Defects in LMAN1 are THE cause of factor V and factor VIII combined deficiency type 1 (F5F8D1) [MIM:[http://omim.org/entry/227300 227300]]; also known as multiple coagulation factor deficiency I (MCFD1). F5F8D1 is an autosomal recessive blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:10090935</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] Defects in MCFD2 are a cause of factor V and factor VIII combined deficiency type 2 (F5F8D2) [MIM:[http://omim.org/entry/613625 613625]]; also known as multiple coagulation factor deficiency 2 (MCFD2). F5F8D2 is a blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.<ref>PMID:12717434</ref> <ref>PMID:18590741</ref>

-	~~Authors~~: ~~Satoh, T~~., ~~Suzuki~~, K., ~~Kato~~, K.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/LMAN1_HUMAN LMAN1_HUMAN]] Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.<ref>PMID:13130098</ref> <ref>PMID:12717434</ref> [[http://www.uniprot.org/uniprot/MCFD2_HUMAN MCFD2_HUMAN]] The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.<ref>PMID:12717434</ref>

-	~~Description: Crystal~~ structure ~~of ERGIC~~-53/~~MCFD2~~, Calcium-~~free form~~	+	==About this Structure==
		+	[[3wht]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHT OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Kato, K.]]
		+	[[Category: Satoh, T.]]
		+	[[Category: Suzuki, K.]]
		+	[[Category: Beta-sandwich]]
		+	[[Category: Calcium binding]]
		+	[[Category: Cargo receptor]]
		+	[[Category: Ef-hand]]
		+	[[Category: Er]]
		+	[[Category: Ergic]]
		+	[[Category: Protein transport]]

OCA at 06:28, 2 October 2013

OCA — Wed, 02 Oct 2013 06:28:29 GMT

←Older revision		Revision as of 06:28, 2 October 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3wht is ON HOLD	+	The entry 3wht is ON HOLD until Paper Publication

	Authors: Satoh, T., Suzuki, K., Kato, K.		Authors: Satoh, T., Suzuki, K., Kato, K.

	Description: Crystal structure of ERGIC-53/MCFD2, Calcium-free form		Description: Crystal structure of ERGIC-53/MCFD2, Calcium-free form

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

OCA — Thu, 12 Sep 2013 04:26:51 GMT

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

←Older revision

Revision as of 04:26, 12 September 2013

OCA: New page: '''Unreleased structure''' The entry 3wht is ON HOLD Authors: Satoh, T., Suzuki, K., Kato, K. Description: Crystal structure of ERGIC-53/MCFD2, Calcium-free form

OCA — Thu, 12 Sep 2013 04:26:50 GMT

New page: '''Unreleased structure''' The entry 3wht is ON HOLD Authors: Satoh, T., Suzuki, K., Kato, K. Description: Crystal structure of ERGIC-53/MCFD2, Calcium-free form

New page

'''Unreleased structure'''

The entry 3wht is ON HOLD

Authors: Satoh, T., Suzuki, K., Kato, K.

Description: Crystal structure of ERGIC-53/MCFD2, Calcium-free form