4na9 - Revision history

OCA at 06:50, 3 April 2024

OCA — Wed, 03 Apr 2024 06:50:39 GMT

←Older revision		Revision as of 06:50, 3 April 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4na9]] 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=4NA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NA9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4na9]] 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=4NA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NA9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1T7:3-AMINO-5-[(2S,4R)-6-CARBAMIMIDOYL-4-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-2-YL]BIPHENYL-2-CARBOXYLIC+ACID'>1T7</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.24Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1T7:3-AMINO-5-[(2S,4R)-6-CARBAMIMIDOYL-4-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-2-YL]BIPHENYL-2-CARBOXYLIC+ACID'>1T7</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4na9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na9 OCA], [https://pdbe.org/4na9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4na9 RCSB], [https://www.ebi.ac.uk/pdbsum/4na9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4na9 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=4na9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na9 OCA], [https://pdbe.org/4na9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4na9 RCSB], [https://www.ebi.ac.uk/pdbsum/4na9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4na9 ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.		[https://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Antithrombotic agents that are inhibitors of factor XIa (FXIa) have the potential to demonstrate robust efficacy with a low bleeding risk profile. Herein, we describe a series of tetrahydroquinoline (THQ) derivatives as FXIa inhibitors. Compound 1 was identified as a potent and selective tool compound for proof of concept studies. It exhibited excellent antithrombotic efficacy in rabbit thrombosis models and did not prolong bleeding times. This demonstrates proof of concept for the FXIa mechanism in animal models with a reversible, small molecule inhibitor.

-	Tetrahydroquinoline Derivatives as Potent and Selective Factor XIa Inhibitors.,Quan ML, Wong PC, Wang C, Woerner F, Smallheer JM, Barbera FA, Bozarth JM, Brown RL, Harpel MR, Luettgen JM, Morin PE, Peterson T, Ramamurthy V, Rendina AR, Rossi KA, Watson CA, Wei A, Zhang G, Seiffert D, Wexler RR J Med Chem. 2014 Jan 17. PMID:24405333<ref>PMID:24405333</ref>	+	==See Also==
-		+	*[[Factor VIIa 3D structures\|Factor VIIa 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 4na9" style~~=~~"background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:16, 11 January 2023

OCA — Wed, 11 Jan 2023 08:16:51 GMT

←Older revision		Revision as of 08:16, 11 January 2023
Line 1:		Line 1:

	==Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid==		==Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid==
-	<StructureSection load='4na9' size='340' side='right' caption='[[4na9]], [[Resolution\|resolution]] 2.24Å' scene=''>	+	<StructureSection load='4na9' size='340' side='right'caption='[[4na9]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4na9]] 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=4NA9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NA9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4na9]] 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=4NA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NA9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1T7:3-AMINO-5-[(2S,4R)-6-CARBAMIMIDOYL-4-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-2-YL]BIPHENYL-2-CARBOXYLIC+ACID'>1T7</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1T7:3-AMINO-5-[(2S,4R)-6-CARBAMIMIDOYL-4-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-2-YL]BIPHENYL-2-CARBOXYLIC+ACID'>1T7</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">F7 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4na9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na9 OCA], [https://pdbe.org/4na9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4na9 RCSB], [https://www.ebi.ac.uk/pdbsum/4na9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4na9 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/Coagulation_factor_VIIa Coagulation factor VIIa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.21 3.4.21.21] </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=4na9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na9 OCA], [~~http~~://pdbe.org/4na9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4na9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4na9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4na9 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Defects in F7 are the cause of factor VII deficiency (FA7D) [MIM:[~~http~~://omim.org/entry/227500 227500]]. A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.<ref>PMID:8043443</ref> <ref>PMID:2070047</ref> <ref>PMID:1634227</ref> <ref>PMID:8364544</ref> <ref>PMID:8204879</ref> <ref>PMID:7981691</ref> <ref>PMID:7974346</ref> <ref>PMID:8652821</ref> <ref>PMID:8844208</ref> <ref>PMID:8940045</ref> <ref>PMID:8883260</ref> <ref>PMID:9414278</ref> <ref>PMID:9576180</ref> <ref>PMID:9452082</ref> <ref>PMID:11091194</ref> <ref>PMID:11129332</ref> <ref>PMID:10862079</ref> <ref>PMID:12472587</ref> <ref>PMID:14717781</ref> <ref>PMID:19751712</ref> <ref>PMID:18976247</ref> <ref>PMID:19432927</ref> <ref>PMID:21206266</ref> <ref>PMID:21372693</ref>	+	[https://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN] Defects in F7 are the cause of factor VII deficiency (FA7D) [MIM:[https://omim.org/entry/227500 227500]. A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.<ref>PMID:8043443</ref> <ref>PMID:2070047</ref> <ref>PMID:1634227</ref> <ref>PMID:8364544</ref> <ref>PMID:8204879</ref> <ref>PMID:7981691</ref> <ref>PMID:7974346</ref> <ref>PMID:8652821</ref> <ref>PMID:8844208</ref> <ref>PMID:8940045</ref> <ref>PMID:8883260</ref> <ref>PMID:9414278</ref> <ref>PMID:9576180</ref> <ref>PMID:9452082</ref> <ref>PMID:11091194</ref> <ref>PMID:11129332</ref> <ref>PMID:10862079</ref> <ref>PMID:12472587</ref> <ref>PMID:14717781</ref> <ref>PMID:19751712</ref> <ref>PMID:18976247</ref> <ref>PMID:19432927</ref> <ref>PMID:21206266</ref> <ref>PMID:21372693</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.	+	[https://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Coagulation factor VIIa~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Wei, A]]	+	[[Category: Wei A]]
-	~~[[Category: Blood coagulation factor]]~~	+
-	~~[[Category: Calcium-binding]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Plasma]]~~	+
-	~~[[Category: Protein inhibitor complex]]~~	+
-	~~[[Category: Serine protease~~]]	+

OCA at 14:26, 11 August 2016

OCA — Thu, 11 Aug 2016 14:26:08 GMT

←Older revision		Revision as of 14:26, 11 August 2016
Line 1:		Line 1:
		+
	==Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid==		==Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid==
	<StructureSection load='4na9' size='340' side='right' caption='[[4na9]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='4na9' size='340' side='right' caption='[[4na9]], [[Resolution\|resolution]] 2.24Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">F7 ([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">F7 ([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/Coagulation_factor_VIIa Coagulation factor VIIa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.21 3.4.21.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_VIIa Coagulation factor VIIa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.21 3.4.21.21] </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=4na9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4na9 RCSB], [http://www.ebi.ac.uk/pdbsum/4na9 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=4na9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na9 OCA], [http://pdbe.org/4na9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4na9 RCSB], [http://www.ebi.ac.uk/pdbsum/4na9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4na9 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 4na9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:42, 5 January 2015

OCA — Mon, 05 Jan 2015 08:42:09 GMT

←Older revision		Revision as of 08:42, 5 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4na9\| PDB=4na9 \| SCENE= }}~~	+	==Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid==
-	===Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid===	+	<StructureSection load='4na9' size='340' side='right' caption='[[4na9]], [[Resolution\|resolution]] 2.24Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24405333}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4na9]] 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=4NA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NA9 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1T7:3-AMINO-5-[(2S,4R)-6-CARBAMIMIDOYL-4-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-2-YL]BIPHENYL-2-CARBOXYLIC+ACID'>1T7</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">F7 ([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/Coagulation_factor_VIIa Coagulation factor VIIa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.21 3.4.21.21] </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=4na9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4na9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4na9 RCSB], [http://www.ebi.ac.uk/pdbsum/4na9 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Defects in F7 are the cause of factor VII deficiency (FA7D) [MIM:[http://omim.org/entry/227500 227500]]. A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.<ref>PMID:8043443</ref> <ref>PMID:2070047</ref> <ref>PMID:1634227</ref> <ref>PMID:8364544</ref> <ref>PMID:8204879</ref> <ref>PMID:7981691</ref> <ref>PMID:7974346</ref> <ref>PMID:8652821</ref> <ref>PMID:8844208</ref> <ref>PMID:8940045</ref> <ref>PMID:8883260</ref> <ref>PMID:9414278</ref> <ref>PMID:9576180</ref> <ref>PMID:9452082</ref> <ref>PMID:11091194</ref> <ref>PMID:11129332</ref> <ref>PMID:10862079</ref> <ref>PMID:12472587</ref> <ref>PMID:14717781</ref> <ref>PMID:19751712</ref> <ref>PMID:18976247</ref> <ref>PMID:19432927</ref> <ref>PMID:21206266</ref> <ref>PMID:21372693</ref>		[[http://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Defects in F7 are the cause of factor VII deficiency (FA7D) [MIM:[http://omim.org/entry/227500 227500]]. A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.<ref>PMID:8043443</ref> <ref>PMID:2070047</ref> <ref>PMID:1634227</ref> <ref>PMID:8364544</ref> <ref>PMID:8204879</ref> <ref>PMID:7981691</ref> <ref>PMID:7974346</ref> <ref>PMID:8652821</ref> <ref>PMID:8844208</ref> <ref>PMID:8940045</ref> <ref>PMID:8883260</ref> <ref>PMID:9414278</ref> <ref>PMID:9576180</ref> <ref>PMID:9452082</ref> <ref>PMID:11091194</ref> <ref>PMID:11129332</ref> <ref>PMID:10862079</ref> <ref>PMID:12472587</ref> <ref>PMID:14717781</ref> <ref>PMID:19751712</ref> <ref>PMID:18976247</ref> <ref>PMID:19432927</ref> <ref>PMID:21206266</ref> <ref>PMID:21372693</ref>
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.		[[http://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Antithrombotic agents that are inhibitors of factor XIa (FXIa) have the potential to demonstrate robust efficacy with a low bleeding risk profile. Herein, we describe a series of tetrahydroquinoline (THQ) derivatives as FXIa inhibitors. Compound 1 was identified as a potent and selective tool compound for proof of concept studies. It exhibited excellent antithrombotic efficacy in rabbit thrombosis models and did not prolong bleeding times. This demonstrates proof of concept for the FXIa mechanism in animal models with a reversible, small molecule inhibitor.

-	~~==About this Structure==~~	+	Tetrahydroquinoline Derivatives as Potent and Selective Factor XIa Inhibitors.,Quan ML, Wong PC, Wang C, Woerner F, Smallheer JM, Barbera FA, Bozarth JM, Brown RL, Harpel MR, Luettgen JM, Morin PE, Peterson T, Ramamurthy V, Rendina AR, Rossi KA, Watson CA, Wei A, Zhang G, Seiffert D, Wexler RR J Med Chem. 2014 Jan 17. PMID:24405333<ref>PMID:24405333</ref>
-	~~[[4na9]] is a 2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4NA9 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024405333</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Coagulation factor VIIa]]		[[Category: Coagulation factor VIIa]]
-	[[Category: Wei, A.]]	+	[[Category: Human]]
		+	[[Category: Wei, A]]
	[[Category: Blood coagulation factor]]		[[Category: Blood coagulation factor]]
	[[Category: Calcium-binding]]		[[Category: Calcium-binding]]

OCA at 05:02, 13 February 2014

OCA — Thu, 13 Feb 2014 05:02:51 GMT

←Older revision		Revision as of 05:02, 13 February 2014
Line 1:		Line 1:
-	''~~'Unreleased structure'''~~	+	{{STRUCTURE_4na9\| PDB=4na9 \| SCENE= }}
		+	===Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid===
		+	{{ABSTRACT_PUBMED_24405333}}

-	~~The~~ entry ~~4na9 is ON HOLD~~ ~~until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Defects in F7 are the cause of factor VII deficiency (FA7D) [MIM:[http://omim.org/entry/227500 227500]]. A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.<ref>PMID:8043443</ref> <ref>PMID:2070047</ref> <ref>PMID:1634227</ref> <ref>PMID:8364544</ref> <ref>PMID:8204879</ref> <ref>PMID:7981691</ref> <ref>PMID:7974346</ref> <ref>PMID:8652821</ref> <ref>PMID:8844208</ref> <ref>PMID:8940045</ref> <ref>PMID:8883260</ref> <ref>PMID:9414278</ref> <ref>PMID:9576180</ref> <ref>PMID:9452082</ref> <ref>PMID:11091194</ref> <ref>PMID:11129332</ref> <ref>PMID:10862079</ref> <ref>PMID:12472587</ref> <ref>PMID:14717781</ref> <ref>PMID:19751712</ref> <ref>PMID:18976247</ref> <ref>PMID:19432927</ref> <ref>PMID:21206266</ref> <ref>PMID:21372693</ref>

-	~~Authors~~: ~~Wei~~, A.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/FA7_HUMAN FA7_HUMAN]] Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.

-	~~Description~~: ~~Factor VIIa in complex with the inhibitor 3'-amino-5'~~-[~~(2s~~,~~4r)~~-~~6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl~~]~~biphenyl~~-~~2-carboxylic acid~~	+	==About this Structure==
		+	[[4na9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NA9 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:024405333</ref><references group="xtra"/><references/>
		+	[[Category: Coagulation factor VIIa]]
		+	[[Category: Wei, A.]]
		+	[[Category: Blood coagulation factor]]
		+	[[Category: Calcium-binding]]
		+	[[Category: Glycoprotein]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Plasma]]
		+	[[Category: Protein inhibitor complex]]
		+	[[Category: Serine protease]]

OCA at 09:11, 8 January 2014

OCA — Wed, 08 Jan 2014 09:11:14 GMT

←Older revision		Revision as of 09:11, 8 January 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4na9 is ON HOLD	+	The entry 4na9 is ON HOLD until Paper Publication

-	Authors: Wei, A~~., Sheriff, S~~.	+	Authors: Wei, A.

-	Description: Factor VIIa in complex with the inhibitor 3'-amino-5'-(~~(2S~~, 4R)-6-carbamimidoyl-4-phenyl-1,2,3,4-~~tetrahydro~~-2-~~quinolinyl)~~-2-~~biphenylcarboxylic~~ acid	+	Description: Factor VIIa in complex with the inhibitor 3'-amino-5'-[(2s,4r)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydroquinolin-2-yl]biphenyl-2-carboxylic acid

OCA at 07:42, 13 November 2013

OCA — Wed, 13 Nov 2013 07:42:05 GMT

←Older revision		Revision as of 07:42, 13 November 2013
Line 5:		Line 5:
	Authors: Wei, A., Sheriff, S.		Authors: Wei, A., Sheriff, S.

-	Description: ~~FACTOR VIIA IN COMPLEX WITH THE INHIBITOR~~ 3'-~~AMINO~~-5'-((2S, 4R)-6-~~CARBAMIMIDOYL~~-4-~~PHENYL~~-1,2,3,4-~~TETRAHYDRO~~-2-~~QUINOLINYL~~)-2-~~BIPHENYLCARBOXYLIC ACID~~	+	Description: Factor VIIa in complex with the inhibitor 3'-amino-5'-((2S, 4R)-6-carbamimidoyl-4-phenyl-1,2,3,4-tetrahydro-2-quinolinyl)-2-biphenylcarboxylic acid

OCA: Protected "4na9" [edit=sysop:move=sysop]

OCA — Wed, 06 Nov 2013 07:05:49 GMT

Protected "4na9" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:05, 6 November 2013

OCA: New page: '''Unreleased structure''' The entry 4na9 is ON HOLD Authors: Wei, A., Sheriff, S. Description: FACTOR VIIA IN COMPLEX WITH THE INHIBITOR 3'-AMINO-5'-((2S, 4R)-6-CARBAMIMIDOYL-4-PHENYL...

OCA — Wed, 06 Nov 2013 07:05:48 GMT

New page: '''Unreleased structure''' The entry 4na9 is ON HOLD Authors: Wei, A., Sheriff, S. Description: FACTOR VIIA IN COMPLEX WITH THE INHIBITOR 3'-AMINO-5'-((2S, 4R)-6-CARBAMIMIDOYL-4-PHENYL...

New page

'''Unreleased structure'''

The entry 4na9 is ON HOLD

Authors: Wei, A., Sheriff, S.

Description: FACTOR VIIA IN COMPLEX WITH THE INHIBITOR 3'-AMINO-5'-((2S, 4R)-6-CARBAMIMIDOYL-4-PHENYL-1,2,3,4-TETRAHYDRO-2-QUINOLINYL)-2-BIPHENYLCARBOXYLIC ACID