4jqg - Revision history

OCA at 15:46, 20 September 2023

OCA — Wed, 20 Sep 2023 15:46:59 GMT

←Older revision		Revision as of 15:46, 20 September 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4jqg]] is a 4 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=4JQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JQG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4jqg]] is a 4 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=4JQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JQG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8MC:(7-METHOXY-2-OXO-2H-CHROMEN-4-YL)ACETIC+ACID'>8MC</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DNW:3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE'>DNW</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PFF:4-FLUORO-L-PHENYLALANINE'>PFF</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</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]] 1.849Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8MC:(7-METHOXY-2-OXO-2H-CHROMEN-4-YL)ACETIC+ACID'>8MC</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DNW:3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE'>DNW</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PFF:4-FLUORO-L-PHENYLALANINE'>PFF</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqg OCA], [https://pdbe.org/4jqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jqg RCSB], [https://www.ebi.ac.uk/pdbsum/4jqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jqg 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=4jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqg OCA], [https://pdbe.org/4jqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jqg RCSB], [https://www.ebi.ac.uk/pdbsum/4jqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jqg ProSAT]</span></td></tr>
	</table>		</table>

OCA at 11:30, 24 November 2022

OCA — Thu, 24 Nov 2022 11:30:23 GMT

←Older revision		Revision as of 11:30, 24 November 2022
Line 1:		Line 1:

	==Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.==		==Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.==
-	<StructureSection load='4jqg' size='340' side='right' caption='[[4jqg]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='4jqg' size='340' side='right'caption='[[4jqg]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4jqg]] is a 4 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=4JQG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4JQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4jqg]] is a 4 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=4JQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JQG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~AZI~~:~~AZIDE~~+~~ION~~'>~~AZI~~</scene>, <scene name='pdbligand=CA:~~CALCIUM~~+ION'>CA</scene>, <scene name='pdbligand=~~EDO~~:~~1,2-ETHANEDIOL~~'>~~EDO~~</scene>, <scene name='pdbligand=~~GOL~~:~~GLYCEROL~~'>~~GOL~~</scene>, <scene name='pdbligand=NA:~~SODIUM+ION~~'>NA</scene>, <scene name='pdbligand=~~PGO~~:~~S-1,2-PROPANEDIOL~~'>~~PGO~~</scene>, <scene name='pdbligand=SR:~~STRONTIUM~~+ION'>SR</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=8MC:(7-METHOXY-2-OXO-2H-CHROMEN-4-YL)ACETIC+ACID'>8MC</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DNW:3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE'>DNW</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PFF:4-FLUORO-L-PHENYLALANINE'>PFF</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=~~8MC~~:(7-~~METHOXY~~-2-~~OXO-2H-CHROMEN-4-YL)ACETIC+ACID~~'>~~8MC~~</scene>, <scene name='pdbligand=~~DNW~~:3-[(2,4-~~DINITROPHENYL)AMINO]-L-ALANINE~~'>~~DNW~~</scene>, <scene name='pdbligand=~~NH2~~:~~AMINO~~+~~GROUP~~'>~~NH2~~</scene>, <scene name='pdbligand=~~PFF~~:~~4-FLUORO-L-PHENYLALANINE~~'>~~PFF~~</scene~~></td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqg OCA], [https://pdbe.org/4jqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jqg RCSB], [https://www.ebi.ac.uk/pdbsum/4jqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jqg ProSAT]</span></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jij\|4jij]], [[4h3x\|4h3x]], [[4h1q\|4h1q]], [[4h2e\|4h2e]], [[4hma\|4hma]], [[4h82\|4h82]], [[2ow0\|2ow0]], [[2ow1\|2ow1]], [[4jxa\|4jxa]]</td></tr>	+
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CLG4B, MMP9 ([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/Gelatinase_B Gelatinase B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.35 3.4.24.35] </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=4jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqg OCA], [~~http~~://pdbe.org/4jqg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4jqg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4jqg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4jqg ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:[~~http~~://omim.org/entry/603932 603932]]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.<ref>PMID:18455130</ref> Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [MIM:[~~http~~://omim.org/entry/613073 613073]]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.	+	[https://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN] Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:[https://omim.org/entry/603932 603932]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.<ref>PMID:18455130</ref> Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [MIM:[https://omim.org/entry/613073 613073]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-\|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.<ref>PMID:1480034</ref>	+	[https://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN] May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-\|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.<ref>PMID:1480034</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4jqg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4jqg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Matrix metalloproteinase 3D structures\|Matrix metalloproteinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Gelatinase B~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Amoura, M]]	+	[[Category: Amoura M]]
-	[[Category: Cassar-Lajeunesse, E]]	+	[[Category: Cassar-Lajeunesse E]]
-	[[Category: Dive, V]]	+	[[Category: Dive V]]
-	[[Category: Stura~~, E A~~]]	+	[[Category: Stura EA]]
-	[[Category: Tranchant, I]]	+	[[Category: Tranchant I]]
-	[[Category: Vera, L]]	+	[[Category: Vera L]]
-	~~[[Category: Catalytic domain]]~~	+
-	~~[[Category: Collagenase]]~~	+
-	~~[[Category: Gelatinase]]~~	+
-	~~[[Category: Halogen-water-hydrogen bridge]]~~	+
-	~~[[Category: Hydrolase-substrate complex]]~~	+
-	~~[[Category: Zincin-like~~]]	+

OCA at 14:11, 15 November 2017

OCA — Wed, 15 Nov 2017 14:11:00 GMT

←Older revision		Revision as of 14:11, 15 November 2017
Line 24:		Line 24:
	</div>		</div>
	<div class="pdbe-citations 4jqg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4jqg" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:36, 11 August 2016

OCA — Thu, 11 Aug 2016 10:36:42 GMT

←Older revision		Revision as of 10:36, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.==		==Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.==
	<StructureSection load='4jqg' size='340' side='right' caption='[[4jqg]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='4jqg' size='340' side='right' caption='[[4jqg]], [[Resolution\|resolution]] 1.85Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CLG4B, MMP9 ([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">CLG4B, MMP9 ([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/Gelatinase_B Gelatinase B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.35 3.4.24.35] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gelatinase_B Gelatinase B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.35 3.4.24.35] </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=4jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jqg RCSB], [http://www.ebi.ac.uk/pdbsum/4jqg 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=4jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqg OCA], [http://pdbe.org/4jqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jqg RCSB], [http://www.ebi.ac.uk/pdbsum/4jqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jqg ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 22:		Line 23:
	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 4jqg" style="background-color:#fffaf0;"></div>

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

OCA at 11:51, 20 January 2015

OCA — Tue, 20 Jan 2015 11:51:11 GMT

←Older revision		Revision as of 11:51, 20 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4jqg\| PDB=4jqg \| SCENE= }}~~	+	==Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.==
-	===Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.===	+	<StructureSection load='4jqg' size='340' side='right' caption='[[4jqg]], [[Resolution\|resolution]] 1.85Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24583051}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4jqg]] is a 4 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=4JQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JQG FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=8MC:(7-METHOXY-2-OXO-2H-CHROMEN-4-YL)ACETIC+ACID'>8MC</scene>, <scene name='pdbligand=DNW:3-[(2,4-DINITROPHENYL)AMINO]-L-ALANINE'>DNW</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PFF:4-FLUORO-L-PHENYLALANINE'>PFF</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jij\|4jij]], [[4h3x\|4h3x]], [[4h1q\|4h1q]], [[4h2e\|4h2e]], [[4hma\|4hma]], [[4h82\|4h82]], [[2ow0\|2ow0]], [[2ow1\|2ow1]], [[4jxa\|4jxa]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CLG4B, MMP9 ([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/Gelatinase_B Gelatinase B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.35 3.4.24.35] </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=4jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jqg RCSB], [http://www.ebi.ac.uk/pdbsum/4jqg PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:[http://omim.org/entry/603932 603932]]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.<ref>PMID:18455130</ref> Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [MIM:[http://omim.org/entry/613073 613073]]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.		[[http://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:[http://omim.org/entry/603932 603932]]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.<ref>PMID:18455130</ref> Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [MIM:[http://omim.org/entry/613073 613073]]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-\|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.<ref>PMID:1480034</ref>		[[http://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-\|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.<ref>PMID:1480034</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Matrix metalloproteinases (MMPs) are a large family of zinc-dependent endoproteases that catalyze cleavage of extracellular matrix and nonmatrix proteins. MMPs play a role in tissue remodeling, and their uncontrolled activity is associated with number of diseases, including tumor metastasis. Thus, there is a need to develop methods to monitor MMP activity, and number of probes has been previously described. The key problem many probes encounter is the issue of selectivity, since 23 human MMPs, despite playing different physiological roles, have structurally similar active sites. Here, we introduce the halogen bonding concept into the probe design and show that the probe containing iodine exhibits an unprecedented selectivity for MMP-9. We provide structure-based explanation for the selectivity, confirming that it is due to formation of the halogen bond that supports catalysis, and we highlight the value of exploring halogen bonding in the context of selective probe design.

-	~~==About this Structure==~~	+	Halogen Bonding Controls Selectivity of FRET Substrate Probes for MMP-9.,Tranchant I, Vera L, Czarny B, Amoura M, Cassar E, Beau F, Stura EA, Dive V Chem Biol. 2014 Feb 25. pii: S1074-5521(14)00031-3. doi:, 10.1016/j.chembiol.2014.01.008. PMID:24583051<ref>PMID:24583051</ref>
-	~~[[4jqg]] is a 4 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=4JQG OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]		*[[Matrix metalloproteinase\|Matrix metalloproteinase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024583051</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Gelatinase B]]		[[Category: Gelatinase B]]
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Amoura, M.]]	+	[[Category: Amoura, M]]
-	[[Category: Cassar-Lajeunesse, E.]]	+	[[Category: Cassar-Lajeunesse, E]]
-	[[Category: Dive, V.]]	+	[[Category: Dive, V]]
-	[[Category: Stura, E A.]]	+	[[Category: Stura, E A]]
-	[[Category: Tranchant, I.]]	+	[[Category: Tranchant, I]]
-	[[Category: Vera, L.]]	+	[[Category: Vera, L]]
	[[Category: Catalytic domain]]		[[Category: Catalytic domain]]
	[[Category: Collagenase]]		[[Category: Collagenase]]

OCA at 08:23, 16 April 2014

OCA — Wed, 16 Apr 2014 08:23:21 GMT

←Older revision		Revision as of 08:23, 16 April 2014
Line 10:		Line 10:

	==About this Structure==		==About this Structure==
-	[[4jqg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JQG OCA].	+	[[4jqg]] is a 4 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=4JQG OCA].
		+
		+	==See Also==
		+	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:024583051</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024583051</ref><references group="xtra"/><references/>
	[[Category: Gelatinase B]]		[[Category: Gelatinase B]]
		+	[[Category: Human]]
	[[Category: Amoura, M.]]		[[Category: Amoura, M.]]
	[[Category: Cassar-Lajeunesse, E.]]		[[Category: Cassar-Lajeunesse, E.]]

OCA at 13:46, 12 March 2014

OCA — Wed, 12 Mar 2014 13:46:30 GMT

←Older revision		Revision as of 13:46, 12 March 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4jqg\| PDB=4jqg \| SCENE= }}
		+	===Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.===
		+	{{ABSTRACT_PUBMED_24583051}}

-	~~The~~ entry ~~4jqg~~ is ~~ON HOLD until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:[http://omim.org/entry/603932 603932]]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.<ref>PMID:18455130</ref> Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [MIM:[http://omim.org/entry/613073 613073]]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.

-	~~Authors~~: ~~Stura, E~~.A.~~, Vera, L~~.~~, Cassar~~-~~Lajeunesse, E~~.~~, Tranchant, I., Amoura, M., Dive,~~ V.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/MMP9_HUMAN MMP9_HUMAN]] May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-\|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.<ref>PMID:1480034</ref>

-	~~Description: Crystal~~ structure ~~of an inactive mutant of MMP~~-~~9 catalytic~~ domain ~~in complex with a fluorogenic synthetic peptidic~~ substrate ~~with a fluorine atom.~~	+	==About this Structure==
		+	[[4jqg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JQG OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:024583051</ref><references group="xtra"/><references/>
		+	[[Category: Gelatinase B]]
		+	[[Category: Amoura, M.]]
		+	[[Category: Cassar-Lajeunesse, E.]]
		+	[[Category: Dive, V.]]
		+	[[Category: Stura, E A.]]
		+	[[Category: Tranchant, I.]]
		+	[[Category: Vera, L.]]
		+	[[Category: Catalytic domain]]
		+	[[Category: Collagenase]]
		+	[[Category: Gelatinase]]
		+	[[Category: Halogen-water-hydrogen bridge]]
		+	[[Category: Hydrolase-substrate complex]]
		+	[[Category: Zincin-like]]

OCA at 06:50, 16 May 2013

OCA — Thu, 16 May 2013 06:50:59 GMT

←Older revision		Revision as of 06:50, 16 May 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4jqg is ON HOLD	+	The entry 4jqg is ON HOLD until Paper Publication

-	Authors: Stura, E.A., Vera, L.., Cassar-Lajeunesse, E., Tranchant, I., Amoura, M., Dive, V.	+	Authors: Stura, E.A., Vera, L., Cassar-Lajeunesse, E., Tranchant, I., Amoura, M., Dive, V.

	Description: Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.		Description: Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.

OCA: Protected "4jqg" [edit=sysop:move=sysop]

OCA — Wed, 27 Mar 2013 08:22:56 GMT

Protected "4jqg" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:22, 27 March 2013

OCA: New page: '''Unreleased structure''' The entry 4jqg is ON HOLD Authors: Stura, E.A., Vera, L.., Cassar-Lajeunesse, E., Tranchant, I., Amoura, M., Dive, V. Description: Crystal structure of an in...

OCA — Wed, 27 Mar 2013 08:22:54 GMT

New page: '''Unreleased structure''' The entry 4jqg is ON HOLD Authors: Stura, E.A., Vera, L.., Cassar-Lajeunesse, E., Tranchant, I., Amoura, M., Dive, V. Description: Crystal structure of an in...

New page

'''Unreleased structure'''

The entry 4jqg is ON HOLD

Authors: Stura, E.A., Vera, L.., Cassar-Lajeunesse, E., Tranchant, I., Amoura, M., Dive, V.

Description: Crystal structure of an inactive mutant of MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate with a fluorine atom.