9api - Revision history

OCA at 15:03, 6 November 2024

2024-11-06T15:03:21Z

← Older revision		Revision as of 15:03, 6 November 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/9api_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/9api_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 12:25, 10 January 2024

2024-01-10T12:25:19Z

← Older revision		Revision as of 12:25, 10 January 2024
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	==THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM==		==THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM==
	<StructureSection load='9api' size='340' side='right' caption='[[9api]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='9api' size='340' side='right'caption='[[9api]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[9api]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=9API FirstGlance]. <br>		<table><tr><td colspan='2'>[[9api]] 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=9API OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9API FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 3Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[7api\|7api]], [[8api\|8api]]~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=9api FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9api OCA], [~~http~~://pdbe.org/9api PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=9api RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/9api PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=9api 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=9api FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9api OCA], [https://pdbe.org/9api PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9api RCSB], [https://www.ebi.ac.uk/pdbsum/9api PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9api 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]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/9api_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/9api_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 33:		Line 33:

	==See Also==		==See Also==
	*[[Alpha-1-antitrypsin\|Alpha-1-antitrypsin]]		*[[Alpha-1-antitrypsin 3D structures\|Alpha-1-antitrypsin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Deisenhofer, J]]		[[Category: Homo sapiens]]
	[[Category: Huber, R]]		[[Category: Large Structures]]
	[[Category: Loebermann, H]]		[[Category: Deisenhofer J]]
	[[Category: Tokuoka, R]]		[[Category: Huber R]]
	~~[[Category: Proteinase inhibitor~~]]		[[Category: Loebermann H]]
			[[Category: Tokuoka R]]

OCA at 11:46, 5 August 2016

2016-08-05T11:46:26Z

← Older revision		Revision as of 11:46, 5 August 2016
Line 1:		Line 1:

	==THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM==		==THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM==
	<StructureSection load='9api' size='340' side='right' caption='[[9api]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='9api' size='340' side='right' caption='[[9api]], [[Resolution\|resolution]] 3.00Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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">[[7api\|7api]], [[8api\|8api]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[7api\|7api]], [[8api\|8api]]</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=9api FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9api OCA], [http://www.rcsb.org/pdb/explore.do?structureId=9api RCSB], [http://www.ebi.ac.uk/pdbsum/9api 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=9api FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9api OCA], [http://pdbe.org/9api PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=9api RCSB], [http://www.ebi.ac.uk/pdbsum/9api PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=9api ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	<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=9api ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		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 9api" style="background-color:#fffaf0;"></div>

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

OCA at 15:06, 21 December 2014

2014-12-21T15:06:20Z

← Older revision		Revision as of 15:06, 21 December 2014
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	~~{{STRUCTURE_9api\| PDB=9api \| SCENE= }}~~		==THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM==
	===THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM===		<StructureSection load='9api' size='340' side='right' caption='[[9api]], [[Resolution\|resolution]] 3.00Å' scene=''>
	~~{{ABSTRACT_PUBMED_2785270}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[9api]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=9API FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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">[[7api\|7api]], [[8api\|8api]]</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=9api FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9api OCA], [http://www.rcsb.org/pdb/explore.do?structureId=9api RCSB], [http://www.ebi.ac.uk/pdbsum/9api 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/ap/9api_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 ==
			The S variant of the human alpha 1-antitrypsin with E-264----V, is responsible for a mild alpha 1-antitrypsin deficiency quite common in the European population. S protein specifically cleaved at the susceptible peptide bond was crystallized and its crystal structure determined and refined to 3.1 A resolution. The S variant crystallizes isomorphous to the normal M variant. The difference Fourier electron density map shows the E----V change as outstanding residual density. In addition, small structural changes of the main polypeptide chain radiate from the site of mutation and affect parts far removed from it. By the mutation, internal hydrogen bonds and salt linkages of E-264 to Y-38 and K-487, respectively, are lost. They cause the far-reaching slight distortions and are probably related to the reduced thermal stability of the S mutant. They may also be responsible for slower folding of the polypeptide chain and the clinical symptoms of alpha 1-antitrypsin deficiency. In a theoretical study by molecular dynamics methods simulations of the M and S proteins were made and the results analysed with respect to structural and dynamic properties and compared with the experimental results. There is a significant correlation between experimental and theoretical results in some respects.

	~~==Disease==~~		The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism.,Engh R, Lobermann H, Schneider M, Wiegand G, Huber R, Laurell CB Protein Eng. 1989 Mar;2(6):407-15. PMID:2785270<ref>PMID:2785270</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==~~
	~~[[9api]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA].~~

	==See Also==		==See Also==
	*[[Alpha-1-antitrypsin\|Alpha-1-antitrypsin]]		*[[Alpha-1-antitrypsin\|Alpha-1-antitrypsin]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:002785270</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
	[[Category: Deisenhofer, J.]]		</StructureSection>
	[[Category: Huber, R.]]		[[Category: Deisenhofer, J]]
	[[Category: Loebermann, H.]]		[[Category: Huber, R]]
	[[Category: Tokuoka, R.]]		[[Category: Loebermann, H]]
			[[Category: Tokuoka, R]]
	[[Category: Proteinase inhibitor]]		[[Category: Proteinase inhibitor]]

OCA at 21:37, 24 March 2013

2013-03-24T21:37:12Z

← Older revision		Revision as of 21:37, 24 March 2013
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	~~[[Image:9api.png\|left\|200px]]~~

	{{STRUCTURE_9api\| PDB=9api \| SCENE= }}		{{STRUCTURE_9api\| PDB=9api \| SCENE= }}
			===THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM===
			{{ABSTRACT_PUBMED_2785270}}

	===~~THE S VARIANT OF HUMAN ALPHA1~~-~~ANTITRYPSIN~~, ~~STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM===~~		==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>

	~~{{ABSTRACT_PUBMED_2785270}}~~		==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:002785270</ref><references group="xtra"/>		<ref group="xtra">PMID:002785270</ref><references group="xtra"/><references/>
	[[Category: Deisenhofer, J.]]		[[Category: Deisenhofer, J.]]
	[[Category: Huber, R.]]		[[Category: Huber, R.]]

OCA at 20:02, 20 October 2012

2012-10-20T20:02:40Z

← Older revision		Revision as of 20:02, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[9api]] is a 2 chain structure ~~of [[Alpha-1-antitrypsin]]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA].		[[9api]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA].

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

OCA: Protected "9api" [edit=sysop:move=sysop]

2012-07-27T09:14:23Z

Protected "9api" [edit=sysop:move=sysop]

← Older revision	Revision as of 09:14, 27 July 2012
(No difference)

OCA at 09:14, 27 July 2012

2012-07-27T09:14:21Z

← Older revision		Revision as of 09:14, 27 July 2012
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	~~{{Seed}}~~
	[[Image:9api.png\|left\|200px]]		[[Image:9api.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_9api", 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_9api\| PDB=9api \| SCENE= }}		{{STRUCTURE_9api\| PDB=9api \| SCENE= }}

	===THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM===		===THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM===


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	==About this Structure==		==About this Structure==
	~~9API~~ is a 2 ~~chains~~ structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA].		[[9api]] is a 2 chain structure of [[Alpha-1-antitrypsin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA].

			==See Also==
			*[[Alpha-1-antitrypsin\|Alpha-1-antitrypsin]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~2785270~~</ref><references group="xtra"/>		<ref group="xtra">PMID:002785270</ref><references group="xtra"/>
	[[Category: Deisenhofer, J.]]		[[Category: Deisenhofer, J.]]
	[[Category: Huber, R.]]		[[Category: Huber, R.]]
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	[[Category: Tokuoka, R.]]		[[Category: Tokuoka, R.]]
	[[Category: Proteinase inhibitor]]		[[Category: Proteinase inhibitor]]

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2009-02-18T00:36:37Z

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	==About this Structure==		==About this Structure==
	9API is a ~~[[Single protein]]~~ structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA].		9API is a 2 chains structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9API OCA].

	==Reference==		==Reference==
	The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism., Engh R, Lobermann H, Schneider M, Wiegand G, Huber R, Laurell CB, Protein Eng. 1989 Mar;2(6):407-15. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~2785270 2785270]~~		<ref group="xtra">PMID:2785270</ref><references group="xtra"/>
	~~[[Category: Single protein]]~~
	[[Category: Deisenhofer, J.]]		[[Category: Deisenhofer, J.]]
	[[Category: Huber, R.]]		[[Category: Huber, R.]]
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	[[Category: Proteinase inhibitor]]		[[Category: Proteinase inhibitor]]

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			[[Image:9api.png\|left\|200px]]

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	{{STRUCTURE_9api\| PDB=9api \| SCENE= }}		{{STRUCTURE_9api\| PDB=9api \| SCENE= }}

	~~'''~~THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM~~'''~~		===THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM===


	~~==Overview==~~		<!--
	The ~~S variant of the human alpha 1-antitrypsin with E-264----V~~, ~~is responsible for a mild alpha 1-antitrypsin deficiency quite common in the European population. S protein specifically cleaved at~~ the ~~susceptible peptide bond was crystallized and its crystal structure determined and refined to 3.1 A resolution. The S variant crystallizes isomorphous~~ to the ~~normal M variant~~. ~~The difference Fourier electron density map shows the E----V change as outstanding residual density~~. ~~In addition~~, ~~small structural changes of the main polypeptide chain radiate from~~ the ~~site of mutation and affect parts far removed from it~~. ~~By the mutation, internal hydrogen bonds and salt linkages of E~~-~~264 to Y~~-38 and K-487, respectively, are lost. They cause the far-reaching slight distortions and are probably related to the reduced thermal stability of the S mutant. They may also be responsible for slower folding of the polypeptide chain and the clinical symptoms of alpha 1-antitrypsin deficiency. In a theoretical study by molecular dynamics methods simulations of the M and S proteins were made and the results analysed with respect to structural and dynamic properties and compared with the experimental results. There is a significant correlation between experimental and theoretical results in some respects.		The line below this paragraph, {{ABSTRACT_PUBMED_2785270}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 2785270 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_2785270}}

	==About this Structure==		==About this Structure==
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	[[Category: Tokuoka, R.]]		[[Category: Tokuoka, R.]]
	[[Category: Proteinase inhibitor]]		[[Category: Proteinase inhibitor]]
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