1aos - Revision history

OCA at 06:32, 7 February 2024

OCA — Wed, 07 Feb 2024 06:32:32 GMT

←Older revision		Revision as of 06:32, 7 February 2024
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	<StructureSection load='1aos' size='340' side='right'caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>		<StructureSection load='1aos' size='340' side='right'caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aos]] is a 2 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aos]] 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOS FirstGlance]. <br>
-	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~=~~'plainlinks'~~>[~~https://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase~~]~~, with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=~~4.3.2~~.1 4.3.2.1] </span>~~</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]] 4.2Å</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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [https://pdbe.org/1aos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [https://www.ebi.ac.uk/pdbsum/1aos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aos 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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [https://pdbe.org/1aos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [https://www.ebi.ac.uk/pdbsum/1aos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aos ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[https://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>	+	[https://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[https://omim.org/entry/207900 207900]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1aos 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=1aos ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Intragenic complementation has been observed at the argininosuccinate lyase (ASL) locus. Intragenic complementation is a phenomenon that occurs when a multimeric protein is formed from subunits produced by different mutant alleles of a gene. The resulting hybrid protein exhibits enzymatic activity that is greater than that found in the oligomeric proteins produced by each mutant allele alone. The mutations involved in the most successful complementation event observed in ASL deficiency were found to be an aspartate to glycine mutation at codon 87 of one allele (D87G) coupled with a glutamine to arginine mutation at codon 286 of the other (Q286R). To understand the structural basis of the Q286R:D87G intragenic complementation event at the ASL locus, we have determined the x-ray crystal structure of recombinant human ASL at 4. 0 A resolution. The structure has been refined to an R factor of 18. 8%. Two monomers related by a noncrystallographic 2-fold axis comprise the asymmetric unit, and a crystallographic 2-fold axis of space group P3121 completes the tetramer. Each of the four active sites is composed of residues from three monomers. Structural mapping of the Q286R and D87G mutations indicate that both are near the active site and each is contributed by a different monomer. Thus when mutant monomers combine randomly such that one active site contains both mutations, it is required by molecular symmetry that another active site exists with no mutations. These "native" active sites give rise to the observed partial recovery of enzymatic activity.
-
-	Human argininosuccinate lyase: a structural basis for intragenic complementation.,Turner MA, Simpson A, McInnes RR, Howell PL Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9063-8. PMID:9256435<ref>PMID:9256435</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1aos" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Argininosuccinate lyase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Howell~~, P L~~]]	+	[[Category: Howell PL]]
-	[[Category: Mcinnes~~, R R~~]]	+	[[Category: Mcinnes RR]]
-	[[Category: Simpson, A]]	+	[[Category: Simpson A]]
-	[[Category: Turner~~, M A]]~~	+	[[Category: Turner MA]]
-	~~[[Category: Arginine biosynthesis]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Urea cycle~~]]	+

OCA at 09:47, 26 May 2021

OCA — Wed, 26 May 2021 09:47:30 GMT

←Older revision		Revision as of 09:47, 26 May 2021
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	<StructureSection load='1aos' size='340' side='right'caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>		<StructureSection load='1aos' size='340' side='right'caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aos]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1AOS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aos]] is a 2 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOS FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [~~http~~://pdbe.org/1aos PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1aos PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1aos 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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [https://pdbe.org/1aos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [https://www.ebi.ac.uk/pdbsum/1aos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aos ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[~~http~~://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>	+	[[https://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[https://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:47, 21 August 2019

OCA — Wed, 21 Aug 2019 07:47:25 GMT

←Older revision		Revision as of 07:47, 21 August 2019
Line 1:		Line 1:

	==HUMAN ARGININOSUCCINATE LYASE==		==HUMAN ARGININOSUCCINATE LYASE==
-	<StructureSection load='1aos' size='340' side='right' caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>	+	<StructureSection load='1aos' size='340' side='right'caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1aos]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aos]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aos_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aos_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:
	[[Category: Argininosuccinate lyase]]		[[Category: Argininosuccinate lyase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Howell, P L]]		[[Category: Howell, P L]]
	[[Category: Mcinnes, R R]]		[[Category: Mcinnes, R R]]

OCA at 10:46, 15 November 2017

OCA — Wed, 15 Nov 2017 10:46:05 GMT

←Older revision		Revision as of 10:46, 15 November 2017
Line 1:		Line 1:
		+
	==HUMAN ARGININOSUCCINATE LYASE==		==HUMAN ARGININOSUCCINATE LYASE==
	<StructureSection load='1aos' size='340' side='right' caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>		<StructureSection load='1aos' size='340' side='right' caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1aos]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aos]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [http://pdbe.org/1aos PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [http://www.ebi.ac.uk/pdbsum/1aos 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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [http://pdbe.org/1aos PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [http://www.ebi.ac.uk/pdbsum/1aos PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aos ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 10:22, 9 February 2016

OCA — Tue, 09 Feb 2016 10:22:26 GMT

←Older revision		Revision as of 10:22, 9 February 2016
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	<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=1aos ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:19, 10 September 2015

OCA — Thu, 10 Sep 2015 21:19:18 GMT

←Older revision		Revision as of 21:19, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1aos' size='340' side='right' caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>		<StructureSection load='1aos' size='340' side='right' caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aos]] 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aos]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [http://www.ebi.ac.uk/pdbsum/1aos 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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [http://pdbe.org/1aos PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [http://www.ebi.ac.uk/pdbsum/1aos PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 26:		Line 26:
	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 1aos" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 31:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Argininosuccinate lyase]]		[[Category: Argininosuccinate lyase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Howell, P L]]		[[Category: Howell, P L]]
	[[Category: Mcinnes, R R]]		[[Category: Mcinnes, R R]]

OCA at 06:14, 25 December 2014

OCA — Thu, 25 Dec 2014 06:14:09 GMT

←Older revision		Revision as of 06:14, 25 December 2014
Line 8:		Line 8:
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[http://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>		[[http://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[http://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>
-	== Function ==
-
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:16, 22 December 2014

OCA — Mon, 22 Dec 2014 11:16:17 GMT

←Older revision		Revision as of 11:16, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1aos]] 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aos]] 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span></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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [http://www.ebi.ac.uk/pdbsum/1aos 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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [http://www.ebi.ac.uk/pdbsum/1aos PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[http://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>		[[http://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[http://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>
Line 34:		Line 34:
	[[Category: Argininosuccinate lyase]]		[[Category: Argininosuccinate lyase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Howell, P L.]]	+	[[Category: Howell, P L]]
-	[[Category: Mcinnes, R R.]]	+	[[Category: Mcinnes, R R]]
-	[[Category: Simpson, A.]]	+	[[Category: Simpson, A]]
-	[[Category: Turner, M A.]]	+	[[Category: Turner, M A]]
	[[Category: Arginine biosynthesis]]		[[Category: Arginine biosynthesis]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Urea cycle]]		[[Category: Urea cycle]]

OCA at 17:10, 29 September 2014

OCA — Mon, 29 Sep 2014 17:10:30 GMT

←Older revision		Revision as of 17:10, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1aos\| PDB~~=1aos \| ~~SCENE~~= }}	+	==HUMAN ARGININOSUCCINATE LYASE==
-	===~~HUMAN ARGININOSUCCINATE LYASE~~===	+	<StructureSection load='1aos' size='340' side='right' caption='[[1aos]], [[Resolution\|resolution]] 4.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_9256435}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1aos]] 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=1AOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOS FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span></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=1aos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aos RCSB], [http://www.ebi.ac.uk/pdbsum/1aos PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[http://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref> <ref>PMID:2263616</ref> <ref>PMID:12408190</ref> <ref>PMID:17326097</ref>
		+	== Function ==

-	==~~Disease~~==	+	== Evolutionary Conservation ==
-	[[~~http~~://~~www~~.~~uniprot~~.~~org~~/~~uniprot~~/~~ARLY_HUMAN ARLY_HUMAN~~]~~] Defects in ASL are~~ the ~~cause of arginosuccinic aciduria (ARGINSA)~~ [~~MIM:~~[http://~~omim~~.~~org~~/~~entry~~/~~207900 207900]~~]. ~~An autosomal recessive disorder of~~ the ~~urea cycle~~. The ~~disease~~ is ~~characterized~~ by ~~mental and physical retardation~~, ~~liver enlargement~~, ~~skin lesions, dry~~ and ~~brittle hair showing trichorrhexis nodosa microscopically~~ and ~~fluorescing red, convulsions,~~ and ~~episodic unconsciousness~~.~~<ref>PMID:1705937</ref><ref>PMID:2263616</ref><ref>PMID:12408190</ref><ref>PMID:17326097</ref>~~	+	[[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/ao/1aos_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 ==
		+	Intragenic complementation has been observed at the argininosuccinate lyase (ASL) locus. Intragenic complementation is a phenomenon that occurs when a multimeric protein is formed from subunits produced by different mutant alleles of a gene. The resulting hybrid protein exhibits enzymatic activity that is greater than that found in the oligomeric proteins produced by each mutant allele alone. The mutations involved in the most successful complementation event observed in ASL deficiency were found to be an aspartate to glycine mutation at codon 87 of one allele (D87G) coupled with a glutamine to arginine mutation at codon 286 of the other (Q286R). To understand the structural basis of the Q286R:D87G intragenic complementation event at the ASL locus, we have determined the x-ray crystal structure of recombinant human ASL at 4. 0 A resolution. The structure has been refined to an R factor of 18. 8%. Two monomers related by a noncrystallographic 2-fold axis comprise the asymmetric unit, and a crystallographic 2-fold axis of space group P3121 completes the tetramer. Each of the four active sites is composed of residues from three monomers. Structural mapping of the Q286R and D87G mutations indicate that both are near the active site and each is contributed by a different monomer. Thus when mutant monomers combine randomly such that one active site contains both mutations, it is required by molecular symmetry that another active site exists with no mutations. These "native" active sites give rise to the observed partial recovery of enzymatic activity.

-	~~==About this Structure==~~	+	Human argininosuccinate lyase: a structural basis for intragenic complementation.,Turner MA, Simpson A, McInnes RR, Howell PL Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9063-8. PMID:9256435<ref>PMID:9256435</ref>
-	~~[[1aos]] 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=1AOS OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:009256435</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Argininosuccinate lyase]]		[[Category: Argininosuccinate lyase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 06:14, 25 March 2013

OCA — Mon, 25 Mar 2013 06:14:27 GMT

←Older revision		Revision as of 06:14, 25 March 2013
Line 1:		Line 1:
-	[[Image:1aos.png\|left\|200px]]
-
	{{STRUCTURE_1aos\| PDB=1aos \| SCENE= }}		{{STRUCTURE_1aos\| PDB=1aos \| SCENE= }}
-
	===HUMAN ARGININOSUCCINATE LYASE===		===HUMAN ARGININOSUCCINATE LYASE===
		+	{{ABSTRACT_PUBMED_9256435}}

-	~~{{ABSTRACT_PUBMED_9256435}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ARLY_HUMAN ARLY_HUMAN]] Defects in ASL are the cause of arginosuccinic aciduria (ARGINSA) [MIM:[http://omim.org/entry/207900 207900]]. An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness.<ref>PMID:1705937</ref><ref>PMID:2263616</ref><ref>PMID:12408190</ref><ref>PMID:17326097</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 10:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:009256435</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009256435</ref><references group="xtra"/><references/>
	[[Category: Argininosuccinate lyase]]		[[Category: Argininosuccinate lyase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]