1gaz - Revision history

OCA at 23:29, 27 December 2023

OCA — Wed, 27 Dec 2023 23:29:13 GMT

←Older revision		Revision as of 23:29, 27 December 2023
Line 3:		Line 3:
	<StructureSection load='1gaz' size='340' side='right'caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1gaz' size='340' side='right'caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NA:SODIUM+ION'>NA</scene>~~</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]] 1.8Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]~~ </~~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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [https://pdbe.org/1gaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [https://www.ebi.ac.uk/pdbsum/1gaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaz 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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [https://pdbe.org/1gaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [https://www.ebi.ac.uk/pdbsum/1gaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>	+	[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.	+	[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 39:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Lysozyme]]~~	+	[[Category: Funahashi J]]
-	[[Category: Funahashi, J]]	+	[[Category: Takano K]]
-	[[Category: Takano, K]]	+	[[Category: Yamagata Y]]
-	[[Category: Yamagata, Y]]	+	[[Category: Yutani K]]
-	[[Category: Yutani, K]]	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Surface mutant~~]]	+

OCA at 07:16, 22 September 2021

OCA — Wed, 22 Sep 2021 07:16:26 GMT

OCA at 14:07, 18 December 2019

OCA — Wed, 18 Dec 2019 14:07:22 GMT

←Older revision		Revision as of 14:07, 18 December 2019
Line 1:		Line 1:

	==Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions==		==Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions==
-	<StructureSection load='1gaz' size='340' side='right' caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1gaz' size='340' side='right'caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>
Line 40:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Funahashi, J]]		[[Category: Funahashi, J]]

OCA at 06:36, 3 January 2018

OCA — Wed, 03 Jan 2018 06:36:13 GMT

←Older revision		Revision as of 06:36, 3 January 2018
Line 1:		Line 1:
		+
	==Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions==		==Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions==
	<StructureSection load='1gaz' size='340' side='right' caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1gaz' size='340' side='right' caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [http://pdbe.org/1gaz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [http://www.ebi.ac.uk/pdbsum/1gaz 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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [http://pdbe.org/1gaz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [http://www.ebi.ac.uk/pdbsum/1gaz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ga/1gaz_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ga/1gaz_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>

OCA at 02:54, 7 February 2016

OCA — Sun, 07 Feb 2016 02:54:14 GMT

←Older revision		Revision as of 02:54, 7 February 2016
Line 20:		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=1gaz ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:58, 9 September 2015

OCA — Wed, 09 Sep 2015 20:58:43 GMT

←Older revision		Revision as of 20:58, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1gaz' size='340' side='right' caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1gaz' size='340' side='right' caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [http://www.ebi.ac.uk/pdbsum/1gaz 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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [http://pdbe.org/1gaz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [http://www.ebi.ac.uk/pdbsum/1gaz PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 1gaz" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Funahashi, J]]		[[Category: Funahashi, J]]

OCA at 18:44, 22 December 2014

OCA — Mon, 22 Dec 2014 18:44:19 GMT

←Older revision		Revision as of 18:44, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [http://www.ebi.ac.uk/pdbsum/1gaz 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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [http://www.ebi.ac.uk/pdbsum/1gaz PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>		[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
Line 39:		Line 39:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
-	[[Category: Funahashi, J.]]	+	[[Category: Funahashi, J]]
-	[[Category: Takano, K.]]	+	[[Category: Takano, K]]
-	[[Category: Yamagata, Y.]]	+	[[Category: Yamagata, Y]]
-	[[Category: Yutani, K.]]	+	[[Category: Yutani, K]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Surface mutant]]		[[Category: Surface mutant]]

OCA at 14:08, 29 September 2014

OCA — Mon, 29 Sep 2014 14:08:33 GMT

←Older revision		Revision as of 14:08, 29 September 2014
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-	~~{{STRUCTURE_1gaz\| PDB=1gaz \| SCENE= }}~~	+	==Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions==
-	===Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions===	+	<StructureSection load='1gaz' size='340' side='right' caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_10913274}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [http://www.ebi.ac.uk/pdbsum/1gaz PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
		+	== 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/ga/1gaz_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 ==
		+	To clarify the role of amino acid residues at turns in the conformational stability and folding of a globular protein, six mutant human lysozymes deleted or substituted at turn structures were investigated by calorimetry, GuHCl denaturation experiments, and X-ray crystal analysis. The thermodynamic properties of the mutant and wild-type human lysozymes were compared and discussed on the basis of their three-dimensional structures. For the deletion mutants, Delta47-48 and Delta101, the deleted residues are in turns on the surface and are absent in human alpha-lactalbumin, which is homologous to human lysozyme in amino acid sequence and tertiary structure. The stability of both mutants would be expected to increase due to a decrease in conformational entropy in the denatured state; however, both proteins were destabilized. The destabilizations were mainly caused by the disappearance of intramolecular hydrogen bonds. Each part deleted was recovered by the turn region like the alpha-lactalbumin structure, but there were differences in the main-chain conformation of the turn between each deletion mutant and alpha-lactalbumin even if the loop length was the same. For the point mutants, R50G, Q58G, H78G, and G37Q, the main-chain conformations of these substitution residues located in turns adopt a left-handed helical region in the wild-type structure. It is thought that the left-handed non-Gly residue has unfavorable conformational energy compared to the left-handed Gly residue. Q58G was stabilized, but the others had little effect on the stability. The structural analysis revealed that the turns could rearrange the main-chain conformation to accommodate the left-handed non-Gly residues. The present results indicate that turn structures are able to change their main-chain conformations, depending upon the side-chain features of amino acid residues on the turns. Furthermore, stopped-flow GuHCl denaturation experiments on the six mutants were performed. The effects of mutations on unfolding-refolding kinetics were significantly different among the mutant proteins. The deletion/substitutions in turns located in the alpha-domain of human lysozyme affected the refolding rate, indicating the contribution of turn structures to the folding of a globular protein.

-	~~==Disease==~~	+	Role of amino acid residues at turns in the conformational stability and folding of human lysozyme.,Takano K, Yamagata Y, Yutani K Biochemistry. 2000 Jul 25;39(29):8655-65. PMID:10913274<ref>PMID:10913274</ref>
-	~~[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects~~ in ~~LYZ are a cause~~ of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme ~~amyloids~~. ~~Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome~~, ~~arterial hypertension~~, ~~hepatosplenomegaly~~, ~~cholestasis, petechial skin rash~~.<ref>PMID:~~8464497~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity~~ of ~~immunoagents~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1gaz]] 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=1GAZ OCA].~~	+

	==See Also==		==See Also==
-	*[[~~Hen Egg-White (HEW)~~ Lysozyme\|~~Hen Egg-White (HEW)~~ Lysozyme]]	+	*[[Lysozyme 3D structures\|Lysozyme 3D structures]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:010913274</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]

OCA at 09:51, 24 March 2013

OCA — Sun, 24 Mar 2013 09:51:17 GMT

←Older revision		Revision as of 09:51, 24 March 2013
Line 1:		Line 1:
-	[[Image:1gaz.png\|left\|200px]]
-
	{{STRUCTURE_1gaz\| PDB=1gaz \| SCENE= }}		{{STRUCTURE_1gaz\| PDB=1gaz \| SCENE= }}
-
	===Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions===		===Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions===
		+	{{ABSTRACT_PUBMED_10913274}}

-	~~{{ABSTRACT_PUBMED_10913274}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010913274</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010913274</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]

OCA at 05:23, 20 October 2012

OCA — Sat, 20 Oct 2012 05:23:44 GMT

←Older revision		Revision as of 05:23, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1gaz]] is a 1 chain structure ~~of [[Hen Egg-White (HEW) Lysozyme]]~~ 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=1GAZ OCA].	+	[[1gaz]] 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=1GAZ OCA].

	==See Also==		==See Also==
Line 14:		Line 14:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010913274~~</ref><ref group="xtra">PMID:011087397~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010913274</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]

←Older revision		Revision as of 07:16, 22 September 2021
Line 3:		Line 3:
	<StructureSection load='1gaz' size='340' side='right'caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1gaz' size='340' side='right'caption='[[1gaz]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gaz]] 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=1GAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mei\|2mei]], [[1gay\|1gay]], [[1gb0\|1gb0]], [[1gb2\|1gb2]], [[1gb3\|1gb3]], [[1gb5\|1gb5]], [[1gb6\|1gb6]], [[1gb7\|1gb7]], [[1gb8\|1gb8]], [[1gb9\|1gb9]], [[1gbo\|1gbo]], [[1gbw\|1gbw]], [[1gbx\|1gbx]], [[1gby\|1gby]], [[1gbz\|1gbz]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [~~http~~://pdbe.org/1gaz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1gaz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaz 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=1gaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gaz OCA], [https://pdbe.org/1gaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gaz RCSB], [https://www.ebi.ac.uk/pdbsum/1gaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gaz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[~~http~~://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>	+	[[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.	+	[[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]