1iz2 - Revision history

OCA at 23:39, 27 December 2023

OCA — Wed, 27 Dec 2023 23:39:35 GMT

←Older revision		Revision as of 23:39, 27 December 2023
Line 3:		Line 3:
	<StructureSection load='1iz2' size='340' side='right'caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1iz2' size='340' side='right'caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1iz2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GLC:ALPHA~~-~~D-GLUCOSE'>GLC</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]] 2.2Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=Z6W:'>Z6W</scene></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=Z6W:(5R)-5-[(2R)-2-hydroxynonyl]-beta-D-xylulofuranose'>Z6W</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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [https://pdbe.org/1iz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1iz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iz2 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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [https://pdbe.org/1iz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1iz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iz2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[https://omim.org/entry/613490 613490]]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>	+	[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[https://omim.org/entry/613490 613490]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref>	+	[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hwang~~, K Y~~]]	+	[[Category: Hwang KY]]
-	[[Category: Im, H]]	+	[[Category: Im H]]
-	[[Category: Woo, M S]]	+	[[Category: Woo M-S]]
-	[[Category: Yu, M H]]	+	[[Category: Yu M-H]]
-	~~[[Category: Antitrypsin]]~~	+
-	~~[[Category: Folding]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Serpin~~]]	+

OCA at 11:08, 4 August 2021

OCA — Wed, 04 Aug 2021 11:08:01 GMT

←Older revision		Revision as of 11:08, 4 August 2021
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	<StructureSection load='1iz2' size='340' side='right'caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1iz2' size='340' side='right'caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1iz2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~SUM~~:2-[~~3,4-DIHYDROXY-2~~-~~HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY~~]~~-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL~~'>~~SUM~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [~~http~~://pdbe.org/1iz2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1iz2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1iz2 ProSAT]</span></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=Z6W:'>Z6W</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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [https://pdbe.org/1iz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1iz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iz2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[~~http~~://omim.org/entry/613490 613490]]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>	+	[[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[https://omim.org/entry/613490 613490]]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref>	+	[[https://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:15, 30 October 2019

OCA — Wed, 30 Oct 2019 10:15:04 GMT

←Older revision		Revision as of 10:15, 30 October 2019
Line 1:		Line 1:

	==Interactions causing the kinetic trap in serpin protein folding==		==Interactions causing the kinetic trap in serpin protein folding==
-	<StructureSection load='1iz2' size='340' side='right' caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='1iz2' size='340' side='right'caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1iz2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1iz2" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Alpha-1-antitrypsin 3D structures\|Alpha-1-antitrypsin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hwang, K Y]]		[[Category: Hwang, K Y]]
	[[Category: Im, H]]		[[Category: Im, H]]

OCA at 09:00, 17 January 2018

OCA — Wed, 17 Jan 2018 09:00:09 GMT

←Older revision		Revision as of 09:00, 17 January 2018
Line 1:		Line 1:
		+
	==Interactions causing the kinetic trap in serpin protein folding==		==Interactions causing the kinetic trap in serpin protein folding==
	<StructureSection load='1iz2' size='340' side='right' caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1iz2' size='340' side='right' caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene></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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://pdbe.org/1iz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1iz2 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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://pdbe.org/1iz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1iz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iz2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iz/1iz2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iz/1iz2_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 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1iz2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1iz2" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Alpha-1-antitrypsin\|Alpha-1-antitrypsin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:17, 8 February 2016

OCA — Mon, 08 Feb 2016 13:17:42 GMT

←Older revision		Revision as of 13:17, 8 February 2016
Line 18:		Line 18:
	<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=1iz2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:56, 10 September 2015

OCA — Thu, 10 Sep 2015 11:56:36 GMT

←Older revision		Revision as of 11:56, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1iz2' size='340' side='right' caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='1iz2' size='340' side='right' caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene></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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1iz2 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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://pdbe.org/1iz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1iz2 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		Line 28:
	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 1iz2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hwang, K Y]]		[[Category: Hwang, K Y]]
	[[Category: Im, H]]		[[Category: Im, H]]

OCA at 12:01, 2 January 2015

OCA — Fri, 02 Jan 2015 12:01:14 GMT

←Older revision		Revision as of 12:01, 2 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene></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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1iz2 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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1iz2 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[http://omim.org/entry/613490 613490]]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>		[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[http://omim.org/entry/613490 613490]]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Hwang, K Y.]]	+	[[Category: Hwang, K Y]]
-	[[Category: Im, H.]]	+	[[Category: Im, H]]
-	[[Category: Woo, M S.]]	+	[[Category: Woo, M S]]
-	[[Category: Yu, M H.]]	+	[[Category: Yu, M H]]
	[[Category: Antitrypsin]]		[[Category: Antitrypsin]]
	[[Category: Folding]]		[[Category: Folding]]
	[[Category: Protein binding]]		[[Category: Protein binding]]
	[[Category: Serpin]]		[[Category: Serpin]]

OCA at 15:07, 29 September 2014

OCA — Mon, 29 Sep 2014 15:07:02 GMT

←Older revision		Revision as of 15:07, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1iz2~~\| ~~PDB~~=1iz2 \| ~~SCENE~~= }}	+	==Interactions causing the kinetic trap in serpin protein folding==
-	===~~Interactions causing~~ the kinetic trap in serpin protein folding~~===~~	+	<StructureSection load='1iz2' size='340' side='right' caption='[[1iz2]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_12244055}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1iz2]] is a 1 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=1IZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IZ2 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene><br>
		+	<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=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1iz2 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[http://omim.org/entry/613490 613490]]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref> <ref>PMID:2390072</ref> <ref>PMID:2227940</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref> <ref>PMID:1406456</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/iz/1iz2_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 ==
		+	Conformational transition is fundamental to the mechanism of functional regulation in proteins, and serpins (serine protease inhibitors) can provide insight into this process. Serpins are metastable in their native forms, and they ordinarily undergo conformational transition to a stable state only when they form a tight complex with target proteases. The metastable native form is thus considered to be a kinetically trapped folding intermediate. We sought to understand the nature of the serpin kinetic trap as a step toward discovering how conformational transition is regulated. We found that mutations of the B/C beta-barrel of native alpha(1)-antitrypsin, a prototypical serpin, allowed conversion of the molecule into a more stable state. A 2.2 A resolution crystal structure of the stable form (PDB code, ) showed that the reactive site loop is inserted into an A beta-sheet, as in the latent plasminogen activator inhibitor-1. Mutational analyses suggest strongly that interactions not found in the final stable form cause the kinetic trap in serpin protein folding.

-	~~==Disease==~~	+	Interactions causing the kinetic trap in serpin protein folding.,Im H, Woo MS, Hwang KY, Yu MH J Biol Chem. 2002 Nov 29;277(48):46347-54. Epub 2002 Sep 18. PMID:12244055<ref>PMID:12244055</ref>
-	~~[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects~~ in ~~SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[http://omim.org/entry/613490 613490]]~~. ~~A disorder whose most common manifestation is emphysema~~, ~~which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease~~, ~~which occurs in children and adults~~, ~~and may result in cirrhosis and liver failure. Environmental factors~~, ~~particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age~~.~~<ref>PMID~~:~~1905728</ref><ref>~~PMID:~~2390072</ref>~~<ref>PMID:~~2227940~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase~~, ~~but it also has~~ a ~~moderate affinity for plasmin and thrombin~~. ~~Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator~~. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref><ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of ~~the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE)~~.~~[:]~~<~~ref~~>~~PMID:1906855~~</~~ref~~>~~<ref>PMID:1406456</ref>~~	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[1iz2]] is a 1 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=1IZ2 OCA].	+

	==See Also==		==See Also==
	*[[Alpha-1-antitrypsin\|Alpha-1-antitrypsin]]		*[[Alpha-1-antitrypsin\|Alpha-1-antitrypsin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:012244055</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hwang, K Y.]]		[[Category: Hwang, K Y.]]

OCA at 16:22, 24 March 2013

OCA — Sun, 24 Mar 2013 16:22:41 GMT

←Older revision		Revision as of 16:22, 24 March 2013
Line 1:		Line 1:
-	[[Image:1iz2.png\|left\|200px]]
-
	{{STRUCTURE_1iz2\| PDB=1iz2 \| SCENE= }}		{{STRUCTURE_1iz2\| PDB=1iz2 \| SCENE= }}
-
	===Interactions causing the kinetic trap in serpin protein folding===		===Interactions causing the kinetic trap in serpin protein folding===
		+	{{ABSTRACT_PUBMED_12244055}}

-	~~{{ABSTRACT_PUBMED_12244055}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [MIM:[http://omim.org/entry/613490 613490]]. A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.<ref>PMID:1905728</ref><ref>PMID:2390072</ref><ref>PMID:2227940</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/A1AT_HUMAN A1AT_HUMAN]] Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.[:]<ref>PMID:1906855</ref><ref>PMID:1406456</ref> Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).[:]<ref>PMID:1906855</ref><ref>PMID:1406456</ref>

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:012244055</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012244055</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hwang, K Y.]]		[[Category: Hwang, K Y.]]

OCA at 10:16, 20 October 2012

OCA — Sat, 20 Oct 2012 10:16:07 GMT

←Older revision		Revision as of 10:16, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1iz2]] is a 1 chain structure ~~of [[Alpha-1-antitrypsin]]~~ 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=1IZ2 OCA].	+	[[1iz2]] is a 1 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=1IZ2 OCA].

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