3s9c - Revision history

OCA at 17:23, 1 November 2023

OCA — Wed, 01 Nov 2023 17:23:36 GMT

←Older revision		Revision as of 17:23, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3s9c' size='340' side='right'caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3s9c' size='340' side='right'caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Daboia_russellii_siamensis~~ Daboia ~~russellii~~ siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S9C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_siamensis Daboia siamensis] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S9C FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC~~</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN~~</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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;'>[[3s9a\|3s9a]]~~, ~~[[3s9b\|3s9b]], [[3sbk\|3sbk]]~~<~~/div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95]~~ </~~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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [https://pdbe.org/3s9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [https://www.ebi.ac.uk/pdbsum/3s9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s9c 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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [https://pdbe.org/3s9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [https://www.ebi.ac.uk/pdbsum/3s9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s9c ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[https://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[https://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref> <ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[https://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref> <ref>PMID:11435304</ref> <ref>PMID:11858490</ref> <ref>PMID:14617013</ref> <ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[https://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[https://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI]] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.<ref>PMID:3053712</ref> [[https://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.	+	[https://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.<ref>PMID:3053712</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: Daboia ~~russellii~~ siamensis]]	+	[[Category: Daboia siamensis]]
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Snake venom factor V activator]]~~	+	[[Category: Ben Ammar Y]]
-	~~[[Category:~~ Ammar, Y ~~Ben~~]]	+	[[Category: Nakayama D]]
-	[[Category: Nakayama, D]]	+	[[Category: Takeda S]]
-	[[Category: Takeda, S]]	+
-	~~[[Category: Double six-stranded beta-barrel]]~~	+
-	~~[[Category: Glycosylation]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Serine proteinase~~]]	+

OCA at 07:47, 29 June 2022

OCA — Wed, 29 Jun 2022 07:47:24 GMT

←Older revision		Revision as of 07:47, 29 June 2022
Line 1:		Line 1:

	==Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V==		==Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V==
-	<StructureSection load='3s9c' size='340' side='right' caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='3s9c' size='340' side='right'caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3S9C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S9C FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=~~NAG~~:~~N-ACETYL-D-GLUCOSAMINE~~'>~~NAG~~</scene>, <scene name='pdbligand=ZN:~~ZINC+ION~~'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3s9a\|3s9a]], [[3s9b\|3s9b]], [[3sbk\|3sbk]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s9a\|3s9a]], [[3s9b\|3s9b]], [[3sbk\|3sbk]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95] </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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [~~http~~://pdbe.org/3s9c PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3s9c PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3s9c 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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [https://pdbe.org/3s9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [https://www.ebi.ac.uk/pdbsum/3s9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s9c ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[~~http~~://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref> <ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[~~http~~://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref> <ref>PMID:11435304</ref> <ref>PMID:11858490</ref> <ref>PMID:14617013</ref> <ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[~~http~~://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[~~http~~://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[~~http~~://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>	+	[[https://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[https://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref> <ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[https://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref> <ref>PMID:11435304</ref> <ref>PMID:11858490</ref> <ref>PMID:14617013</ref> <ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[https://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[https://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI]] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.<ref>PMID:3053712</ref> [[~~http~~://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.	+	[[https://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI]] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.<ref>PMID:3053712</ref> [[https://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:

	==See Also==		==See Also==
-	*[[Proteinase\|Proteinase]]	+	*[[Proteinase 3D structures\|Proteinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Daboia russellii siamensis]]		[[Category: Daboia russellii siamensis]]
		+	[[Category: Large Structures]]
	[[Category: Snake venom factor V activator]]		[[Category: Snake venom factor V activator]]
	[[Category: Ammar, Y Ben]]		[[Category: Ammar, Y Ben]]

OCA at 10:08, 13 February 2019

OCA — Wed, 13 Feb 2019 10:08:22 GMT

←Older revision		Revision as of 10:08, 13 February 2019
Line 3:		Line 3:
	<StructureSection load='3s9c' size='340' side='right' caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3s9c' size='340' side='right' caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Dabsi Dabsi~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S9C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S9C FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:~~ZINC+ION~~'>ZN</scene>, <scene name='pdbligand=~~NAG~~:~~N-ACETYL-D-GLUCOSAMINE~~'>~~NAG~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3s9a\|3s9a]], [[3s9b\|3s9b]], [[3sbk\|3sbk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3s9a\|3s9a]], [[3s9b\|3s9b]], [[3sbk\|3sbk]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95] </span></td></tr>
Line 29:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Dabsi~~]]	+	[[Category: Daboia russellii siamensis]]
	[[Category: Snake venom factor V activator]]		[[Category: Snake venom factor V activator]]
	[[Category: Ammar, Y Ben]]		[[Category: Ammar, Y Ben]]

OCA at 09:49, 4 August 2016

OCA — Thu, 04 Aug 2016 09:49:17 GMT

←Older revision		Revision as of 09:49, 4 August 2016
Line 1:		Line 1:
		+
	==Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V==		==Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V==
	<StructureSection load='3s9c' size='340' side='right' caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='3s9c' size='340' side='right' caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Daboia_russellii_siamensis Daboia russellii siamensis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S9C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dabsi Dabsi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S9C FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3s9a\|3s9a]], [[3s9b\|3s9b]], [[3sbk\|3sbk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3s9a\|3s9a]], [[3s9b\|3s9b]], [[3sbk\|3sbk]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95] </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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [http://www.ebi.ac.uk/pdbsum/3s9c 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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [http://pdbe.org/3s9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [http://www.ebi.ac.uk/pdbsum/3s9c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s9c 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 3s9c" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Daboia russellii siamensis~~]]	+	[[Category: Dabsi]]
	[[Category: Snake venom factor V activator]]		[[Category: Snake venom factor V activator]]
	[[Category: Ammar, Y Ben]]		[[Category: Ammar, Y Ben]]

OCA at 06:37, 21 December 2014

OCA — Sun, 21 Dec 2014 06:37:47 GMT

←Older revision		Revision as of 06:37, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3s9c\| PDB=3s9c \| SCENE= }}~~	+	==Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V==
-	===Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V===	+	<StructureSection load='3s9c' size='340' side='right' caption='[[3s9c]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21871889}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3s9c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S9C FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3s9a\|3s9a]], [[3s9b\|3s9b]], [[3sbk\|3sbk]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Snake_venom_factor_V_activator Snake venom factor V activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.95 3.4.21.95] </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=3s9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s9c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s9c RCSB], [http://www.ebi.ac.uk/pdbsum/3s9c PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[http://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref> <ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[http://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref> <ref>PMID:11435304</ref> <ref>PMID:11858490</ref> <ref>PMID:14617013</ref> <ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[http://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[http://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>		[[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[http://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref> <ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[http://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref> <ref>PMID:11435304</ref> <ref>PMID:11858490</ref> <ref>PMID:14617013</ref> <ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[http://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[http://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI]] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.<ref>PMID:3053712</ref> [[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Russell's viper venom factor V (FV) activator (RVV-V) is a thrombin-like proteinase that specifically cleaves the Arg1545-Ser1546 bond of FV. Here we present the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) determined at 1.8A resolution. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P(7))-Arg1545 (P(1)), of the cleaved substrate. Comparison with substrate-free structures reveals conformational changes of the RVV-V loops upon substrate binding, suggesting that the multiple interactions are mediated by an induced-fit mechanism. The results provide an explanation for the narrow specificity of RVV-V.

-	~~==Function==~~	+	Structural basis of coagulation factor V recognition for cleavage by RVV-V.,Nakayama D, Ben Ammar Y, Miyata T, Takeda S FEBS Lett. 2011 Aug 23. PMID:21871889<ref>PMID:21871889</ref>
-	~~[[http://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI]] Venom serine protease that selectively activates~~ factor V ~~(F5) in a calcium~~-~~independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor~~ V ~~molecule~~. ~~Induces the coagulation of mammalian plasma~~.<ref>PMID:~~3053712~~</ref> [[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3s9c]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:021871889</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Proteinase\|Proteinase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Daboia russellii siamensis]]		[[Category: Daboia russellii siamensis]]
	[[Category: Snake venom factor V activator]]		[[Category: Snake venom factor V activator]]
-	[[Category: Ammar, Y Ben.]]	+	[[Category: Ammar, Y Ben]]
-	[[Category: Nakayama, D.]]	+	[[Category: Nakayama, D]]
-	[[Category: Takeda, S.]]	+	[[Category: Takeda, S]]
	[[Category: Double six-stranded beta-barrel]]		[[Category: Double six-stranded beta-barrel]]
	[[Category: Glycosylation]]		[[Category: Glycosylation]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Serine proteinase]]		[[Category: Serine proteinase]]

OCA at 10:34, 3 July 2013

OCA — Wed, 03 Jul 2013 10:34:51 GMT

←Older revision		Revision as of 10:34, 3 July 2013
Line 4:		Line 4:

	==Disease==		==Disease==
-	[[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[http://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref><ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[http://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref><ref>PMID:11435304</ref><ref>PMID:11858490</ref><ref>PMID:14617013</ref><ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[http://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[http://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>	+	[[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[http://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref> <ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[http://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref> <ref>PMID:11435304</ref> <ref>PMID:11858490</ref> <ref>PMID:14617013</ref> <ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[http://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[http://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>

	==Function==		==Function==
-	[[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.	+	[[http://www.uniprot.org/uniprot/VSPG_DABSI VSPG_DABSI]] Venom serine protease that selectively activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma.<ref>PMID:3053712</ref> [[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.

	==About this Structure==		==About this Structure==
Line 13:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021871889~~</ref><ref group="xtra">PMID:020054136~~</ref><references group="xtra"/><references/>	+	<ref group="xtra">PMID:021871889</ref><references group="xtra"/><references/>
	[[Category: Daboia russellii siamensis]]		[[Category: Daboia russellii siamensis]]
	[[Category: Snake venom factor V activator]]		[[Category: Snake venom factor V activator]]

OCA at 12:06, 24 March 2013

OCA — Sun, 24 Mar 2013 12:06:31 GMT

←Older revision		Revision as of 12:06, 24 March 2013
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-	[[Image:3s9c.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3s9c", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
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	{{STRUCTURE_3s9c\| PDB=3s9c \| SCENE= }}		{{STRUCTURE_3s9c\| PDB=3s9c \| SCENE= }}
-
	===Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V===		===Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V===
		+	{{ABSTRACT_PUBMED_21871889}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:[http://omim.org/entry/227400 227400]]; also known as Owren parahemophilia. It is a hemorrhagic diastesis.<ref>PMID:10942390</ref><ref>PMID:12393490</ref> Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THPH2) [MIM:[http://omim.org/entry/188055 188055]]. THPH2 is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.<ref>PMID:9454742</ref><ref>PMID:11435304</ref><ref>PMID:11858490</ref><ref>PMID:14617013</ref><ref>PMID:14695241</ref> Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome (BDCHS) [MIM:[http://omim.org/entry/600880 600880]]. A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera. Defects in F5 may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in F5 are associated with susceptibility to pregnancy loss, recurrent, type 1 (RPRGL1) [MIM:[http://omim.org/entry/614389 614389]]. RPRGL1 is a common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.<ref>PMID:11018168</ref>

-	~~<!--~~	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21871889}}, adds the Publication Abstract to the page~~	+	[[http://www.uniprot.org/uniprot/FA5_HUMAN FA5_HUMAN]] Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov), where 21871889 is~~ the ~~PubMed ID number~~.	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_21871889}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021871889</ref><ref group="xtra">PMID:020054136</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021871889</ref><ref group="xtra">PMID:020054136</ref><references group="xtra"/><references/>
	[[Category: Daboia russellii siamensis]]		[[Category: Daboia russellii siamensis]]
	[[Category: Snake venom factor V activator]]		[[Category: Snake venom factor V activator]]

OCA at 06:12, 7 September 2011

OCA — Wed, 07 Sep 2011 06:12:06 GMT

←Older revision		Revision as of 06:12, 7 September 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3s9c.jpg\|left\|200px]]

-	The ~~entry 3s9c~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3s9c", 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_3s9c\| PDB=3s9c \| SCENE= }}

-	~~Authors: Nakayama~~, ~~D., Ben Ammar, Y., Takeda, S.~~	+	===Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V===

-	~~Description~~: ~~Russell's viper venom serine proteinase~~, ~~RVV~~-~~V in complex~~ with ~~the fragment (residues 1533~~-~~1546) of human~~ factor V	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21871889}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21871889 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21871889}}
		+
		+	==About this Structure==
		+	[[3s9c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S9C OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021871889</ref><ref group="xtra">PMID:020054136</ref><references group="xtra"/>
		+	[[Category: Daboia russellii siamensis]]
		+	[[Category: Snake venom factor V activator]]
		+	[[Category: Ammar, Y Ben.]]
		+	[[Category: Nakayama, D.]]
		+	[[Category: Takeda, S.]]
		+	[[Category: Double six-stranded beta-barrel]]
		+	[[Category: Glycosylation]]
		+	[[Category: Hydrolase]]
		+	[[Category: Serine proteinase]]

OCA at 06:10, 20 July 2011

OCA — Wed, 20 Jul 2011 06:10:12 GMT

←Older revision		Revision as of 06:10, 20 July 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3s9c is ON HOLD	+	The entry 3s9c is ON HOLD until Paper Publication

	Authors: Nakayama, D., Ben Ammar, Y., Takeda, S.		Authors: Nakayama, D., Ben Ammar, Y., Takeda, S.

	Description: Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V		Description: Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V

OCA at 16:19, 22 June 2011

OCA — Wed, 22 Jun 2011 16:19:29 GMT

←Older revision		Revision as of 16:19, 22 June 2011
Line 3:		Line 3:
	The entry 3s9c is ON HOLD		The entry 3s9c is ON HOLD

-	Authors: Nakayama, D, Ben Ammar, Y, Takeda, S	+	Authors: Nakayama, D., Ben Ammar, Y., Takeda, S.

	Description: Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V		Description: Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V