1dzh - Revision history

OCA at 08:09, 6 December 2023

OCA — Wed, 06 Dec 2023 08:09:37 GMT

←Older revision		Revision as of 08:09, 6 December 2023
Line 3:		Line 3:
	<StructureSection load='1dzh' size='340' side='right'caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>		<StructureSection load='1dzh' size='340' side='right'caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens~~] and [https://en.wikipedia.org/wiki/Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dzh]] 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=1DZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=BMA:BETA~~-~~D-MANNOSE'>BMA</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.85Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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"><div style~~=~~'overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]~~</~~div~~></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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [https://pdbe.org/1dzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [https://www.ebi.ac.uk/pdbsum/1dzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzh 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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [https://pdbe.org/1dzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [https://www.ebi.ac.uk/pdbsum/1dzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[https://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref>	+	[https://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[https://omim.org/entry/613118 613118]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</ref>	+	[https://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 40:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Carrell~~, R W~~]]	+	[[Category: Carrell RW]]
-	[[Category: Huntington~~, J A~~]]	+	[[Category: Huntington JA]]
-	[[Category: Mccoy~~, A J]]~~	+	[[Category: Mccoy AJ]]
-	~~[[Category: Blood clotting]]~~	+
-	~~[[Category: Serpin~~]]	+

OCA at 18:37, 10 March 2021

OCA — Wed, 10 Mar 2021 18:37:47 GMT

←Older revision		Revision as of 18:37, 10 March 2021
Line 3:		Line 3:
	<StructureSection load='1dzh' size='340' side='right'caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>		<StructureSection load='1dzh' size='340' side='right'caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/ ] 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=1DZH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DZH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</div></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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [~~http~~://pdbe.org/1dzh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1dzh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzh 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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [https://pdbe.org/1dzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [https://www.ebi.ac.uk/pdbsum/1dzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[~~http~~://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref>	+	[[https://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[https://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</ref>	+	[[https://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 40:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Carrell, R W]]		[[Category: Carrell, R W]]

OCA at 23:27, 5 June 2019

OCA — Wed, 05 Jun 2019 23:27:20 GMT

←Older revision		Revision as of 23:27, 5 June 2019
Line 1:		Line 1:

	==P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III==		==P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III==
-	<StructureSection load='1dzh' size='340' side='right' caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>	+	<StructureSection load='1dzh' size='340' side='right'caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] 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=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] 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=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>
Line 17:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dz/1dzh_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dz/1dzh_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 34:		Line 34:

	==See Also==		==See Also==
-	*[[Antithrombin\|Antithrombin]]	+	*[[Antithrombin 3D structures\|Antithrombin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
	[[Category: Carrell, R W]]		[[Category: Carrell, R W]]
	[[Category: Huntington, J A]]		[[Category: Huntington, J A]]

OCA at 04:03, 30 August 2017

OCA — Wed, 30 Aug 2017 04:03:26 GMT

←Older revision		Revision as of 04:03, 30 August 2017
Line 1:		Line 1:
		+
	==P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III==		==P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III==
	<StructureSection load='1dzh' size='340' side='right' caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>		<StructureSection load='1dzh' size='340' side='right' caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human Human~~] 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=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] 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=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [http://pdbe.org/1dzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [http://www.ebi.ac.uk/pdbsum/1dzh 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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [http://pdbe.org/1dzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [http://www.ebi.ac.uk/pdbsum/1dzh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dzh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 39:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Human]]
	[[Category: Carrell, R W]]		[[Category: Carrell, R W]]
	[[Category: Huntington, J A]]		[[Category: Huntington, J A]]

OCA at 23:35, 11 September 2015

OCA — Fri, 11 Sep 2015 23:35:52 GMT

←Older revision		Revision as of 23:35, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1dzh' size='340' side='right' caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>		<StructureSection load='1dzh' size='340' side='right' caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [http://www.ebi.ac.uk/pdbsum/1dzh 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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [http://pdbe.org/1dzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [http://www.ebi.ac.uk/pdbsum/1dzh PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 30:
	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 1dzh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Human]]
	[[Category: Carrell, R W]]		[[Category: Carrell, R W]]
	[[Category: Huntington, J A]]		[[Category: Huntington, J A]]

OCA at 21:46, 22 December 2014

OCA — Mon, 22 Dec 2014 21:46:38 GMT

←Older revision		Revision as of 21:46, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [http://www.ebi.ac.uk/pdbsum/1dzh 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=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [http://www.ebi.ac.uk/pdbsum/1dzh PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[http://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref>		[[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[http://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Carrell, R W.]]	+	[[Category: Carrell, R W]]
-	[[Category: Huntington, J A.]]	+	[[Category: Huntington, J A]]
-	[[Category: Mccoy, A J.]]	+	[[Category: Mccoy, A J]]
	[[Category: Blood clotting]]		[[Category: Blood clotting]]
	[[Category: Serpin]]		[[Category: Serpin]]

OCA at 15:51, 29 September 2014

OCA — Mon, 29 Sep 2014 15:51:10 GMT

←Older revision		Revision as of 15:51, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1dzh~~\| ~~PDB~~=1dzh \| ~~SCENE~~= }}	+	==P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III==
-	===~~P14~~-~~FLUORESCEIN~~-~~N135Q~~-~~S380C~~-~~ANTITHROMBIN~~-III===	+	<StructureSection load='1dzh' size='340' side='right' caption='[[1dzh]], [[Resolution\|resolution]] 2.85Å' scene=''>
-	~~{{ABSTRACT_PUBMED_10809774}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZH FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYF:5-[2-(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETYLAMINO]-2-(3,6-DIHYDROXY-9,9A-DIHYDRO-3H-XANTHEN-9-YL)-BENZOIC+ACID'>CYF</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ant\|1ant]], [[1ath\|1ath]], [[2ant\|2ant]], [[1br8\|1br8]], [[1dzg\|1dzg]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dzh RCSB], [http://www.ebi.ac.uk/pdbsum/1dzh PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[http://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref> [:]<ref>PMID:3191114</ref> <ref>PMID:9031473</ref> <ref>PMID:6582486</ref> <ref>PMID:3080419</ref> <ref>PMID:3805013</ref> <ref>PMID:3179438</ref> <ref>PMID:3162733</ref> <ref>PMID:2781509</ref> <ref>PMID:2365065</ref> <ref>PMID:2229057</ref> <ref>PMID:2013320</ref> <ref>PMID:1906811</ref> <ref>PMID:1555650</ref> <ref>PMID:1547341</ref> <ref>PMID:8443391</ref> <ref>PMID:8486379</ref> <ref>PMID:7981186</ref> <ref>PMID:7959685</ref> <ref>PMID:8274732</ref> <ref>PMID:7994035</ref> <ref>PMID:7989582</ref> [:]<ref>PMID:7878627</ref> <ref>PMID:7832187</ref> <ref>PMID:9157604</ref> <ref>PMID:9845533</ref> <ref>PMID:9759613</ref> <ref>PMID:10997988</ref> <ref>PMID:11794707</ref> <ref>PMID:11713457</ref> <ref>PMID:12353073</ref> <ref>PMID:12595305</ref> <ref>PMID:12894857</ref> <ref>PMID:15164384</ref> <ref>PMID:16908819</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dz/1dzh_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Antithrombin is unique among the serpins in that it circulates in a native conformation that is kinetically inactive toward its target proteinase, factor Xa. Activation occurs upon binding of a specific pentasaccharide sequence found in heparin that results in a rearrangement of the reactive center loop removing constraints on the active center P1 residue. We determined the crystal structure of an activated antithrombin variant, N135Q S380C-fluorescein (P14-fluorescein), in order to see how full activation is achieved in the absence of heparin and how the structural effects of the substitution in the hinge region are translated to the heparin binding region. The crystal structure resembles native antithrombin except in the hinge and heparin binding regions. The absence of global conformational change allows for identification of specific interactions, centered on Glu(381) (P13), that are responsible for maintenance of the solution equilibrium between the native and activated forms and establishes the existence of an electrostatic link between the hinge region and the heparin binding region. A revised model for the mechanism of the allosteric activation of antithrombin is proposed.

-	~~==Disease==~~	+	The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions.,Huntington JA, McCoy A, Belzar KJ, Pei XY, Gettins PG, Carrell RW J Biol Chem. 2000 May 19;275(20):15377-83. PMID:10809774<ref>PMID:10809774</ref>
-	~~[[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause~~ of antithrombin ~~III deficiency (AT3D) [MIM:[http://omim~~.~~org/entry/613118 613118]]~~. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-~~binding domain. Type III: alteration~~ of the heparin-binding ~~domain~~. ~~Plasma AT-III antigen levels are normal in type II and III~~. ~~Type IV~~: ~~consists of miscellaneous group of unclassifiable mutations~~.~~<ref>~~PMID:7734359</ref>[:]<ref>PMID:3191114</ref><ref>PMID:9031473</ref><ref>PMID:6582486</ref><ref>PMID:3080419</ref><ref>PMID:3805013</ref><ref>PMID:3179438</ref><ref>PMID:3162733</ref><ref>PMID:2781509</ref><ref>PMID:2365065</ref><ref>PMID:2229057</ref><ref>PMID:2013320</ref><ref>PMID:1906811</ref><ref>PMID:1555650</ref><ref>PMID:1547341</ref><ref>PMID:8443391</ref><ref>PMID:8486379</ref><ref>PMID:7981186</ref><ref>PMID:7959685</ref><ref>PMID:8274732</ref><ref>PMID:7994035</ref><ref>PMID:7989582</ref>[:]<ref>PMID:7878627</ref><ref>PMID:7832187</ref><ref>PMID:9157604</ref><ref>PMID:9845533</ref><ref>PMID:9759613</ref><ref>PMID:10997988</ref><ref>PMID:11794707</ref><ref>PMID:11713457</ref><ref>PMID:12353073</ref><ref>PMID:12595305</ref><ref>PMID:12894857</ref><ref>PMID:15164384</ref><ref>PMID:~~16908819~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates~~ the ~~blood coagulation cascade~~. ~~AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa~~. ~~Its inhibitory activity is greatly enhanced in the presence~~ of ~~heparin~~.<~~ref~~>~~PMID:15853774~~</~~ref~~>	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA].	+

	==See Also==		==See Also==
	*[[Antithrombin\|Antithrombin]]		*[[Antithrombin\|Antithrombin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:010809774</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Carrell, R W.]]		[[Category: Carrell, R W.]]

OCA at 03:13, 25 March 2013

OCA — Mon, 25 Mar 2013 03:13:05 GMT

←Older revision		Revision as of 03:13, 25 March 2013
Line 1:		Line 1:
-	[[Image:1dzh.png\|left\|200px]]
-
	{{STRUCTURE_1dzh\| PDB=1dzh \| SCENE= }}		{{STRUCTURE_1dzh\| PDB=1dzh \| SCENE= }}
-
	===P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III===		===P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III===
		+	{{ABSTRACT_PUBMED_10809774}}

-	~~{{ABSTRACT_PUBMED_10809774}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Defects in SERPINC1 are the cause of antithrombin III deficiency (AT3D) [MIM:[http://omim.org/entry/613118 613118]]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.<ref>PMID:7734359</ref>[:]<ref>PMID:3191114</ref><ref>PMID:9031473</ref><ref>PMID:6582486</ref><ref>PMID:3080419</ref><ref>PMID:3805013</ref><ref>PMID:3179438</ref><ref>PMID:3162733</ref><ref>PMID:2781509</ref><ref>PMID:2365065</ref><ref>PMID:2229057</ref><ref>PMID:2013320</ref><ref>PMID:1906811</ref><ref>PMID:1555650</ref><ref>PMID:1547341</ref><ref>PMID:8443391</ref><ref>PMID:8486379</ref><ref>PMID:7981186</ref><ref>PMID:7959685</ref><ref>PMID:8274732</ref><ref>PMID:7994035</ref><ref>PMID:7989582</ref>[:]<ref>PMID:7878627</ref><ref>PMID:7832187</ref><ref>PMID:9157604</ref><ref>PMID:9845533</ref><ref>PMID:9759613</ref><ref>PMID:10997988</ref><ref>PMID:11794707</ref><ref>PMID:11713457</ref><ref>PMID:12353073</ref><ref>PMID:12595305</ref><ref>PMID:12894857</ref><ref>PMID:15164384</ref><ref>PMID:16908819</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ANT3_HUMAN ANT3_HUMAN]] Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.<ref>PMID:15853774</ref>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010809774</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010809774</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Carrell, R W.]]		[[Category: Carrell, R W.]]

OCA at 21:30, 20 October 2012

OCA — Sat, 20 Oct 2012 21:30:56 GMT

←Older revision		Revision as of 21:30, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1dzh]] is a 2 chain structure ~~of [[Antithrombin]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA].	+	[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA].

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

OCA at 13:29, 27 July 2012

OCA — Fri, 27 Jul 2012 13:29:25 GMT

←Older revision		Revision as of 13:29, 27 July 2012
Line 1:		Line 1:
	[[Image:1dzh.png\|left\|200px]]		[[Image:1dzh.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1dzh", 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_1dzh\| PDB=1dzh \| SCENE= }}		{{STRUCTURE_1dzh\| PDB=1dzh \| SCENE= }}

	===P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III===		===P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_10809774}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 10809774 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_10809774}}		{{ABSTRACT_PUBMED_10809774}}

	==About this Structure==		==About this Structure==
-	[[1dzh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA].	+	[[1dzh]] is a 2 chain structure of [[Antithrombin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZH OCA].
		+
		+	==See Also==
		+	*[[Antithrombin\|Antithrombin]]

	==Reference==		==Reference==
Line 27:		Line 19:
	[[Category: Huntington, J A.]]		[[Category: Huntington, J A.]]
	[[Category: Mccoy, A J.]]		[[Category: Mccoy, A J.]]
		+	[[Category: Blood clotting]]
		+	[[Category: Serpin]]