4e06 - Revision history

OCA at 06:28, 17 October 2024

2024-10-17T06:28:16Z

← Older revision		Revision as of 06:28, 17 October 2024
Line 12:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>		[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Anopheles mosquitoes are vectors of malaria, a potentially fatal blood disease affecting half a billion humans worldwide. These blood-feeding insects include in their antihemostatic arsenal a potent thrombin inhibitor, the flexible and cysteine-less anophelin. Here, we present a thorough structure-and-function analysis of thrombin inhibition by anophelin, including the 2.3-A crystal structure of the human thrombin.anophelin complex. Anophelin residues 32-61 are well-defined by electron density, completely occupying the long cleft between the active site and exosite I. However, in striking contrast to substrates, the D50-R53 anophelin tetrapeptide occupies the active site cleft of the enzyme, whereas the upstream residues A35-P45 shield the regulatory exosite I, defining a unique reverse-binding mode of an inhibitor to the target proteinase. The extensive interactions established, the disruption of thrombin's active site charge-relay system, and the insertion of residue R53 into the proteinase S(1) pocket in an orientation opposed to productive substrates explain anophelin's remarkable specificity and resistance to proteolysis by thrombin. Complementary biophysical and functional characterization of point mutants and truncated versions of anophelin unambiguously establish the molecular mechanism of action of this family of serine proteinase inhibitors (I77). These findings have implications for the design of novel antithrombotics.

			Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector.,Figueiredo AC, de Sanctis D, Gutierrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ Proc Natl Acad Sci U S A. 2012 Dec 26;109(52):E3649-58. doi:, 10.1073/pnas.1211614109. Epub 2012 Dec 5. PMID:23223529<ref>PMID:23223529</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4e06" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 14:48, 14 March 2024

2024-03-14T14:48:54Z

← Older revision		Revision as of 14:48, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e06]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] 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=4E06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E06 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e06]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] 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=4E06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E06 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 3.196Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e06 OCA], [https://pdbe.org/4e06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e06 RCSB], [https://www.ebi.ac.uk/pdbsum/4e06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e06 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=4e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e06 OCA], [https://pdbe.org/4e06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e06 RCSB], [https://www.ebi.ac.uk/pdbsum/4e06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e06 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[https://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 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 F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[https://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[https://omim.org/entry/614390 614390]]. 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:11506076</ref>		[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[https://omim.org/entry/613679 613679]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 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 F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[https://omim.org/entry/188050 188050]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[https://omim.org/entry/614390 614390]. 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:11506076</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>		[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Anopheles mosquitoes are vectors of malaria, a potentially fatal blood disease affecting half a billion humans worldwide. These blood-feeding insects include in their antihemostatic arsenal a potent thrombin inhibitor, the flexible and cysteine-less anophelin. Here, we present a thorough structure-and-function analysis of thrombin inhibition by anophelin, including the 2.3-A crystal structure of the human thrombin.anophelin complex. Anophelin residues 32-61 are well-defined by electron density, completely occupying the long cleft between the active site and exosite I. However, in striking contrast to substrates, the D50-R53 anophelin tetrapeptide occupies the active site cleft of the enzyme, whereas the upstream residues A35-P45 shield the regulatory exosite I, defining a unique reverse-binding mode of an inhibitor to the target proteinase. The extensive interactions established, the disruption of thrombin's active site charge-relay system, and the insertion of residue R53 into the proteinase S(1) pocket in an orientation opposed to productive substrates explain anophelin's remarkable specificity and resistance to proteolysis by thrombin. Complementary biophysical and functional characterization of point mutants and truncated versions of anophelin unambiguously establish the molecular mechanism of action of this family of serine proteinase inhibitors (I77). These findings have implications for the design of novel antithrombotics.

	Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector.,Figueiredo AC, de Sanctis D, Gutierrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ Proc Natl Acad Sci U S A. 2012 Dec 26;109(52):E3649-58. doi:, 10.1073/pnas.1211614109. Epub 2012 Dec 5. PMID:23223529<ref>PMID:23223529</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4e06" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==

OCA at 06:42, 28 September 2022

2022-09-28T06:42:27Z

← Older revision		Revision as of 06:42, 28 September 2022
Line 1:		Line 1:

	==Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism==		==Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism==
	<StructureSection load='4e06' size='340' side='right' caption='[[4e06]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='4e06' size='340' side='right'caption='[[4e06]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e06]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Anoal Anoal~~] and [~~http~~://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E06 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e06]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] 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=4E06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E06 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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">[[4e05\|4e05]]</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=4e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e06 OCA], [https://pdbe.org/4e06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e06 RCSB], [https://www.ebi.ac.uk/pdbsum/4e06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e06 ProSAT]</span></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">anophelin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7167 ANOAL])</td></tr>~~
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </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=4e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e06 OCA], [~~http~~://pdbe.org/4e06 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e06 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e06 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4e06 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[~~http~~://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 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 F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[~~http~~://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[~~http~~://omim.org/entry/614390 614390]]. 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:11506076</ref>		[[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[https://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 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 F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[https://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[https://omim.org/entry/614390 614390]]. 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:11506076</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>		[[https://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:

	==See Also==		==See Also==
	*[[Thrombin\|Thrombin]]		*[[Thrombin 3D Structures\|Thrombin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Anoal~~]]		[[Category: Anopheles albimanus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: ~~Thrombin~~]]		[[Category: Large Structures]]
	[[Category: Cereija~~, T B~~]]		[[Category: Cereija TB]]
	[[Category: Figueiredo~~, A C~~]]		[[Category: Figueiredo AC]]
	[[Category: Fuentes-Prior, P]]		[[Category: Fuentes-Prior P]]
	[[Category: Gutierrez-Gallego, R]]		[[Category: Gutierrez-Gallego R]]
	[[Category: Macedo-Ribeiro, S]]		[[Category: Macedo-Ribeiro S]]
	[[Category: Pereira~~, P J.B~~]]		[[Category: Pereira PJB]]
	[[Category: Sanctis, D ~~de]]~~		[[Category: De Sanctis D]]
	~~[[Category: Hydrolase-hydrolase inhibitor complex~~]]

OCA at 17:39, 5 August 2016

2016-08-05T17:39:08Z

← Older revision		Revision as of 17:39, 5 August 2016
Line 1:		Line 1:

	==Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism==		==Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism==
	<StructureSection load='4e06' size='340' side='right' caption='[[4e06]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='4e06' size='340' side='right' caption='[[4e06]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e06]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Anopheles_albimanus Anopheles albimanus~~] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E06 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e06]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Anoal Anoal] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E06 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=NA:SODIUM+ION'>NA</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">[[4e05\|4e05]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e05\|4e05]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">anophelin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7167 ~~Anopheles albimanus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">anophelin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7167 ANOAL])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </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=4e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e06 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e06 RCSB], [http://www.ebi.ac.uk/pdbsum/4e06 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=4e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e06 OCA], [http://pdbe.org/4e06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e06 RCSB], [http://www.ebi.ac.uk/pdbsum/4e06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e06 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	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 4e06" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 28:		Line 30:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Anopheles albimanus~~]]		[[Category: Anoal]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Thrombin]]		[[Category: Thrombin]]

OCA at 11:26, 21 December 2014

2014-12-21T11:26:08Z

← Older revision		Revision as of 11:26, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4e06\| PDB=4e06 \| SCENE= }}~~		==Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism==
	===Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism===		<StructureSection load='4e06' size='340' side='right' caption='[[4e06]], [[Resolution\|resolution]] 3.20Å' scene=''>
	~~{{ABSTRACT_PUBMED_23223529}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4e06]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E06 FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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">[[4e05\|4e05]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">anophelin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7167 Anopheles albimanus])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </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=4e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e06 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e06 RCSB], [http://www.ebi.ac.uk/pdbsum/4e06 PDBsum]</span></td></tr>
			</table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[http://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref> <ref>PMID:6405779</ref> <ref>PMID:3771562</ref> <ref>PMID:3567158</ref> <ref>PMID:3801671</ref> <ref>PMID:3242619</ref> <ref>PMID:2719946</ref> <ref>PMID:1354985</ref> <ref>PMID:1421398</ref> <ref>PMID:1349838</ref> <ref>PMID:7865694</ref> <ref>PMID:7792730</ref> Genetic variations in F2 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 F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[http://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[http://omim.org/entry/614390 614390]]. 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:11506076</ref>
			== Function ==
			[[http://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Anopheles mosquitoes are vectors of malaria, a potentially fatal blood disease affecting half a billion humans worldwide. These blood-feeding insects include in their antihemostatic arsenal a potent thrombin inhibitor, the flexible and cysteine-less anophelin. Here, we present a thorough structure-and-function analysis of thrombin inhibition by anophelin, including the 2.3-A crystal structure of the human thrombin.anophelin complex. Anophelin residues 32-61 are well-defined by electron density, completely occupying the long cleft between the active site and exosite I. However, in striking contrast to substrates, the D50-R53 anophelin tetrapeptide occupies the active site cleft of the enzyme, whereas the upstream residues A35-P45 shield the regulatory exosite I, defining a unique reverse-binding mode of an inhibitor to the target proteinase. The extensive interactions established, the disruption of thrombin's active site charge-relay system, and the insertion of residue R53 into the proteinase S(1) pocket in an orientation opposed to productive substrates explain anophelin's remarkable specificity and resistance to proteolysis by thrombin. Complementary biophysical and functional characterization of point mutants and truncated versions of anophelin unambiguously establish the molecular mechanism of action of this family of serine proteinase inhibitors (I77). These findings have implications for the design of novel antithrombotics.

	~~==Disease==~~		Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector.,Figueiredo AC, de Sanctis D, Gutierrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ Proc Natl Acad Sci U S A. 2012 Dec 26;109(52):E3649-58. doi:, 10.1073/pnas.1211614109. Epub 2012 Dec 5. PMID:23223529<ref>PMID:23223529</ref>
	[[http://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[http://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by ~~mucocutaneous bleeding symptoms. The severity of~~ the ~~bleeding manifestations correlates with blood factor II levels~~.<ref>PMID:14962227</ref><ref>PMID:6405779</ref><ref>PMID:3771562</ref><ref>PMID:3567158</ref><ref>PMID:3801671</ref><ref>PMID:3242619</ref><ref>PMID:2719946</ref><ref>PMID:1354985</ref><ref>PMID:1421398</ref><ref>PMID:1349838</ref><ref>PMID:7865694</ref><ref>PMID:7792730</ref> Genetic variations in F2 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 F2 are the cause of thrombophilia due to thrombin defect~~ (~~THPH1~~) ~~[MIM:[http~~://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-~~prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis~~. ~~Defects in F2 are associated with susceptibility to pregnancy loss, recurrent~~, ~~type 2 (RPRGL2) [MIM:[http://omim~~.~~org/entry~~/~~614390 614390]]. 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:~~11506076~~</ref>

	~~==Function==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[http:~~/~~/www.uniprot~~.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. ~~Functions in blood homeostasis, inflammation and wound healing~~.<~~ref~~>~~PMID:2856554~~</~~ref~~>		</div>

	==~~About this Structure~~==		==See Also==
	[[~~4e06~~]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA].		*[[Thrombin\|Thrombin]]
			== References ==
	==~~Reference~~==		<references/>
	<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Anopheles albimanus]]		[[Category: Anopheles albimanus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Thrombin]]		[[Category: Thrombin]]
	[[Category: Cereija, T B.]]		[[Category: Cereija, T B]]
	[[Category: Figueiredo, A C.]]		[[Category: Figueiredo, A C]]
	[[Category: Fuentes-Prior, P.]]		[[Category: Fuentes-Prior, P]]
	[[Category: Gutierrez-Gallego, R.]]		[[Category: Gutierrez-Gallego, R]]
	[[Category: Macedo-Ribeiro, S.]]		[[Category: Macedo-Ribeiro, S]]
	[[Category: Pereira, P J.B.]]		[[Category: Pereira, P J.B]]
	[[Category: Sanctis, D de.]]		[[Category: Sanctis, D de]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 02:40, 25 March 2013

2013-03-25T02:40:03Z

← Older revision		Revision as of 02:40, 25 March 2013
Line 1:		Line 1:
	~~[[Image:4e06.png\|left\|200px]]~~

	{{STRUCTURE_4e06\| PDB=4e06 \| SCENE= }}		{{STRUCTURE_4e06\| PDB=4e06 \| SCENE= }}
			===Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism===
			{{ABSTRACT_PUBMED_23223529}}

	===~~Anophelin~~ from the ~~malaria vector inhibits~~ thrombin ~~through~~ a ~~novel reverse~~-~~binding mechanism===~~		==Disease==
			[[http://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Defects in F2 are the cause of factor II deficiency (FA2D) [MIM:[http://omim.org/entry/613679 613679]]. It is a very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.<ref>PMID:14962227</ref><ref>PMID:6405779</ref><ref>PMID:3771562</ref><ref>PMID:3567158</ref><ref>PMID:3801671</ref><ref>PMID:3242619</ref><ref>PMID:2719946</ref><ref>PMID:1354985</ref><ref>PMID:1421398</ref><ref>PMID:1349838</ref><ref>PMID:7865694</ref><ref>PMID:7792730</ref> Genetic variations in F2 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 F2 are the cause of thrombophilia due to thrombin defect (THPH1) [MIM:[http://omim.org/entry/188050 188050]]. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. Note=A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis. Defects in F2 are associated with susceptibility to pregnancy loss, recurrent, type 2 (RPRGL2) [MIM:[http://omim.org/entry/614390 614390]]. 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:11506076</ref>

	~~{{ABSTRACT_PUBMED_23223529}}~~		==Function==
			[[http://www.uniprot.org/uniprot/THRB_HUMAN THRB_HUMAN]] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.<ref>PMID:2856554</ref>

	==About this Structure==		==About this Structure==
	[[4e06]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA].		[[4e06]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA].

			==Reference==
			<references group="xtra"/><references/>
	[[Category: Anopheles albimanus]]		[[Category: Anopheles albimanus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 07:16, 2 January 2013

2013-01-02T07:16:02Z

← Older revision		Revision as of 07:16, 2 January 2013
Line 1:		Line 1:
	[[Image:4e06.~~jpg~~\|left\|200px]]		[[Image:4e06.png\|left\|200px]]

	{{STRUCTURE_4e06\| PDB=4e06 \| SCENE= }}		{{STRUCTURE_4e06\| PDB=4e06 \| SCENE= }}
Line 5:		Line 5:
	===Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism===		===Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism===

			{{ABSTRACT_PUBMED_23223529}}

	==About this Structure==		==About this Structure==

OCA at 10:58, 5 December 2012

2012-12-05T10:58:35Z

← Older revision		Revision as of 10:58, 5 December 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4e06.jpg\|left\|200px]]

	~~The entry~~ 4e06 ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4e06\| PDB=4e06 \| SCENE= }}

	~~Authors: Figueiredo, A.C., de Sanctis, D., Gutierrez~~-~~Gallego, R., Cereija, T.B., Macedo-Ribeiro, S., Fuentes-Prior, P., Pereira, P.J.B.~~		===Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism===

	~~Description~~: ~~Human alpha~~-~~thrombin~~:inhibitor complex
			==About this Structure==
			[[4e06]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_albimanus Anopheles albimanus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E06 OCA].
			[[Category: Anopheles albimanus]]
			[[Category: Homo sapiens]]
			[[Category: Thrombin]]
			[[Category: Cereija, T B.]]
			[[Category: Figueiredo, A C.]]
			[[Category: Fuentes-Prior, P.]]
			[[Category: Gutierrez-Gallego, R.]]
			[[Category: Macedo-Ribeiro, S.]]
			[[Category: Pereira, P J.B.]]
			[[Category: Sanctis, D de.]]
			[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 05:35, 23 May 2012

2012-05-23T05:35:05Z

← Older revision		Revision as of 05:35, 23 May 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e06 is ON HOLD		The entry 4e06 is ON HOLD until Paper Publication

	Authors: Figueiredo, A.C., de Sanctis, D., Gutierrez-Gallego, R., Cereija, T.B., Macedo-Ribeiro, S., Fuentes-Prior, P., Pereira, P.J.B.		Authors: Figueiredo, A.C., de Sanctis, D., Gutierrez-Gallego, R., Cereija, T.B., Macedo-Ribeiro, S., Fuentes-Prior, P., Pereira, P.J.B.

	Description: Human alpha-thrombin:inhibitor complex		Description: Human alpha-thrombin:inhibitor complex

OCA: Protected "4e06" [edit=sysop:move=sysop]

2012-03-14T06:14:36Z

Protected "4e06" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:14, 14 March 2012
(No difference)