3ba0 - Revision history

OCA at 14:42, 1 November 2023

OCA — Wed, 01 Nov 2023 14:42:55 GMT

←Older revision		Revision as of 14:42, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3ba0' size='340' side='right'caption='[[3ba0]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3ba0' size='340' side='right'caption='[[3ba0]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1su3\|1su3]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">MMP12~~, ~~HME ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~<~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65]~~ </~~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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [https://pdbe.org/3ba0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ba0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba0 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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [https://pdbe.org/3ba0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ba0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN]] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.	+	[https://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Macrophage elastase]]~~	+	[[Category: Bertini I]]
-	[[Category: Bertini, I]]	+	[[Category: Calderone V]]
-	[[Category: Calderone, V]]	+	[[Category: Fragai M]]
-	[[Category: Fragai, M]]	+	[[Category: Jaiswal R]]
-	[[Category: Jaiswal, R]]	+	[[Category: Luchinat C]]
-	[[Category: Luchinat, C]]	+	[[Category: Melikian M]]
-	[[Category: Melikian, M]]	+	[[Category: Myonas E]]
-	[[Category: Myonas, E]]	+	[[Category: Svergun DI]]
-	[[Category: Svergun~~, D I]]~~	+
-	~~[[Category: Calcium]]~~	+
-	~~[[Category: Catalytic domain]]~~	+
-	~~[[Category: Domain interaction]]~~	+
-	~~[[Category: Extracellular matrix]]~~	+
-	~~[[Category: Full-length mmp-12]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hemopexin domain]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Metalloprotease]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Secreted]]~~	+
-	~~[[Category: Zinc]]~~	+
-	~~[[Category: Zymogen~~]]	+

OCA at 07:26, 10 November 2021

OCA — Wed, 10 Nov 2021 07:26:02 GMT

←Older revision		Revision as of 07:26, 10 November 2021
Line 1:		Line 1:

	==Crystal structure of full-length human MMP-12==		==Crystal structure of full-length human MMP-12==
-	<StructureSection load='3ba0' size='340' side='right' caption='[[3ba0]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='3ba0' size='340' side='right'caption='[[3ba0]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1su3\|1su3]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1su3\|1su3]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [~~http~~://pdbe.org/3ba0 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ba0 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba0 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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [https://pdbe.org/3ba0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ba0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN]] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.	+	[[https://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN]] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]	+	*[[Matrix metalloproteinase 3D structures\|Matrix metalloproteinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]
	[[Category: Bertini, I]]		[[Category: Bertini, I]]

OCA at 07:54, 18 July 2018

OCA — Wed, 18 Jul 2018 07:54:29 GMT

←Older revision		Revision as of 07:54, 18 July 2018
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/3ba0_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/3ba0_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 48:		Line 48:
	[[Category: Myonas, E]]		[[Category: Myonas, E]]
	[[Category: Svergun, D I]]		[[Category: Svergun, D I]]
		+	[[Category: Calcium]]
	[[Category: Catalytic domain]]		[[Category: Catalytic domain]]
	[[Category: Domain interaction]]		[[Category: Domain interaction]]
Line 57:		Line 58:
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	[[Category: Metalloprotease]]		[[Category: Metalloprotease]]
		+	[[Category: Polymorphism]]
	[[Category: Protease]]		[[Category: Protease]]
	[[Category: Secreted]]		[[Category: Secreted]]
		+	[[Category: Zinc]]
	[[Category: Zymogen]]		[[Category: Zymogen]]

OCA at 07:01, 5 August 2016

OCA — Fri, 05 Aug 2016 07:01:34 GMT

←Older revision		Revision as of 07:01, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of full-length human MMP-12==		==Crystal structure of full-length human MMP-12==
	<StructureSection load='3ba0' size='340' side='right' caption='[[3ba0]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3ba0' size='340' side='right' caption='[[3ba0]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1su3\|1su3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1su3\|1su3]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ba0 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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [http://pdbe.org/3ba0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ba0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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=3ba0 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 3ba0" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]
	[[Category: Bertini, I]]		[[Category: Bertini, I]]

OCA at 16:42, 25 December 2014

OCA — Thu, 25 Dec 2014 16:42:45 GMT

←Older revision		Revision as of 16:42, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1su3\|1su3]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1su3\|1su3]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ba0 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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ba0 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN]] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]
-	[[Category: Bertini, I.]]	+	[[Category: Bertini, I]]
-	[[Category: Calderone, V.]]	+	[[Category: Calderone, V]]
-	[[Category: Fragai, M.]]	+	[[Category: Fragai, M]]
-	[[Category: Jaiswal, R.]]	+	[[Category: Jaiswal, R]]
-	[[Category: Luchinat, C.]]	+	[[Category: Luchinat, C]]
-	[[Category: Melikian, M.]]	+	[[Category: Melikian, M]]
-	[[Category: Myonas, E.]]	+	[[Category: Myonas, E]]
-	[[Category: Svergun, D I.]]	+	[[Category: Svergun, D I]]
	[[Category: Catalytic domain]]		[[Category: Catalytic domain]]
-	[[Category: Domain interaction.]]	+	[[Category: Domain interaction]]
	[[Category: Extracellular matrix]]		[[Category: Extracellular matrix]]
	[[Category: Full-length mmp-12]]		[[Category: Full-length mmp-12]]

OCA at 09:44, 29 September 2014

OCA — Mon, 29 Sep 2014 09:44:05 GMT

←Older revision		Revision as of 09:44, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~3ba0.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of full-length human MMP-12==
		+	<StructureSection load='3ba0' size='340' side='right' caption='[[3ba0]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3ba0]] 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=3BA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BA0 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1su3\|1su3]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </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=3ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ba0 PDBsum]</span></td></tr>
		+	<table>
		+	== 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/ba/3ba0_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 proteolytic activity of matrix metalloproteinases toward extracellular matrix components (ECM), cytokines, chemokines, and membrane receptors is crucial for several homeostatic and pathological processes. Active MMPs are a family of single-chain enzymes (23 family members in the human genome), most of which constituted by a catalytic domain and by a hemopexin-like domain connected by a linker. The X-ray structures of MMP-1 and MMP-2 suggest a conserved and well-defined spatial relationship between the two domains. Here we present structural data for MMP-12, suitably stabilized against self-hydrolysis, both in solution (NMR and SAXS) and in the solid state (X-ray), showing that the hemopexin-like and the catalytic domains experience conformational freedom with respect to each other on a time scale shorter than 10 (-8) s. Hints on the probable conformations are also obtained. This experimental finding opens new perspectives for the often hypothesized active role of the hemopexin-like domain in the enzymatic activity of MMPs.

-	~~{{STRUCTURE_3ba0\| PDB=3ba0 \| SCENE= }}~~	+	Evidence of Reciprocal Reorientation of the Catalytic and Hemopexin-Like Domains of Full-Length MMP-12.,Bertini I, Calderone V, Fragai M, Jaiswal R, Luchinat C, Melikian M, Mylonas E, Svergun DI J Am Chem Soc. 2008 May 9;. PMID:18465858<ref>PMID:18465858</ref>

-	~~===Crystal structure~~ of ~~full-length human MMP-12===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18465858}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3ba0]] 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=3BA0 OCA].~~	+

	==See Also==		==See Also==
-	*[[Elastase\|Elastase]]
	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]		*[[Matrix metalloproteinase\|Matrix metalloproteinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:018465858<~~/~~ref~~><~~ref group="xtra">PMID:015611040</ref><ref group="xtra">PMID:012032297</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]

OCA at 19:02, 20 October 2012

OCA — Sat, 20 Oct 2012 19:02:19 GMT

←Older revision		Revision as of 19:02, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3ba0]] is a 1 chain structure ~~of [[Elastase]] and [[Matrix metalloproteinase]]~~ 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=3BA0 OCA].	+	[[3ba0]] 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=3BA0 OCA].

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

OCA at 06:04, 27 July 2012

OCA — Fri, 27 Jul 2012 06:04:29 GMT

←Older revision		Revision as of 06:04, 27 July 2012
Line 1:		Line 1:
	[[Image:3ba0.png\|left\|200px]]		[[Image:3ba0.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3ba0", 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_3ba0\| PDB=3ba0 \| SCENE= }}		{{STRUCTURE_3ba0\| PDB=3ba0 \| SCENE= }}

	===Crystal structure of full-length human MMP-12===		===Crystal structure of full-length human MMP-12===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18465858}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18465858 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18465858}}		{{ABSTRACT_PUBMED_18465858}}

	==About this Structure==		==About this Structure==
-	[[3ba0]] is a 1 chain structure of [[Elastase]] 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=3BA0 OCA].	+	[[3ba0]] is a 1 chain structure of [[Elastase]] and [[Matrix metalloproteinase]] 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=3BA0 OCA].

	==See Also==		==See Also==
-	*[[Elastase]]	+	*[[Elastase\|Elastase]]
		+	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18465858~~</ref><ref group="xtra">PMID:~~15611040~~</ref><ref group="xtra">PMID:~~12032297~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018465858</ref><ref group="xtra">PMID:015611040</ref><ref group="xtra">PMID:012032297</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]
Line 36:		Line 26:
	[[Category: Myonas, E.]]		[[Category: Myonas, E.]]
	[[Category: Svergun, D I.]]		[[Category: Svergun, D I.]]
-	[[Category: Calcium]]
	[[Category: Catalytic domain]]		[[Category: Catalytic domain]]
	[[Category: Domain interaction.]]		[[Category: Domain interaction.]]
Line 46:		Line 35:
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	[[Category: Metalloprotease]]		[[Category: Metalloprotease]]
-	[[Category: Polymorphism]]
	[[Category: Protease]]		[[Category: Protease]]
	[[Category: Secreted]]		[[Category: Secreted]]
-	[[Category: Zinc]]
	[[Category: Zymogen]]		[[Category: Zymogen]]

OCA: Protected "3ba0" [edit=sysop:move=sysop]

OCA — Sun, 26 Dec 2010 22:39:07 GMT

Protected "3ba0" [edit=sysop:move=sysop]

←Older revision

Revision as of 22:39, 26 December 2010

OCA at 22:39, 26 December 2010

OCA — Sun, 26 Dec 2010 22:39:06 GMT

←Older revision		Revision as of 22:39, 26 December 2010
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3ba0.png\|left\|200px]]		[[Image:3ba0.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~3BA0~~ is a 1 chain structure of 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=3BA0 OCA].	+	[[3ba0]] is a 1 chain structure of [[Elastase]] 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=3BA0 OCA].
		+
		+	==See Also==
		+	*[[Elastase]]

	==Reference==		==Reference==
Line 49:		Line 51:
	[[Category: Zinc]]		[[Category: Zinc]]
	[[Category: Zymogen]]		[[Category: Zymogen]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:03:00 2009''