4h76 - Revision history

OCA at 15:01, 20 September 2023

OCA — Wed, 20 Sep 2023 15:01:13 GMT

←Older revision		Revision as of 15:01, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4h76]] 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=4H76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H76 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4h76]] 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=4H76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H76 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=10B:N-2-(BIPHENYL-4-YLSULFONYL)-N-2-(ISOPROPYLOXY)-ACETOHYDROXAMIC+ACID'>10B</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</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]] 1.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=10B:N-2-(BIPHENYL-4-YLSULFONYL)-N-2-(ISOPROPYLOXY)-ACETOHYDROXAMIC+ACID'>10B</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [https://pdbe.org/4h76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [https://www.ebi.ac.uk/pdbsum/4h76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h76 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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [https://pdbe.org/4h76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [https://www.ebi.ac.uk/pdbsum/4h76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h76 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:03, 3 November 2022

OCA — Thu, 03 Nov 2022 08:03:21 GMT

←Older revision		Revision as of 08:03, 3 November 2022
Line 1:		Line 1:

	==Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor==		==Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor==
-	<StructureSection load='4h76' size='340' side='right' caption='[[4h76]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='4h76' size='340' side='right'caption='[[4h76]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4h76]] 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=4H76 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4H76 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4h76]] 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=4H76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H76 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=10B:N-2-(BIPHENYL-4-YLSULFONYL)-N-2-(ISOPROPYLOXY)-ACETOHYDROXAMIC+ACID'>10B</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</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=10B:N-2-(BIPHENYL-4-YLSULFONYL)-N-2-(ISOPROPYLOXY)-ACETOHYDROXAMIC+ACID'>10B</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</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">[[4h3x\|4h3x]], [[1rmz\|1rmz]], [[4h30\|4h30]], [[4gr0\|4gr0]], [[4gql\|4gql]], [[3lik\|3lik]], [[3ljg\|3ljg]], [[3lil\|3lil]], [[4efs\|4efs]], [[3tsk\|3tsk]], [[3ts4\|3ts4]]</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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [https://pdbe.org/4h76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [https://www.ebi.ac.uk/pdbsum/4h76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h76 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HME, MMP12 ([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='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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [~~http~~://pdbe.org/4h76 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4h76 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4h76 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]	+	*[[Matrix metalloproteinase 3D structures\|Matrix metalloproteinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Macrophage elastase~~]]	+	[[Category: Large Structures]]
-	[[Category: Cassar-Lajeunesse, E]]	+	[[Category: Cassar-Lajeunesse E]]
-	[[Category: Dive, V]]	+	[[Category: Dive V]]
-	[[Category: Nuti, E]]	+	[[Category: Nuti E]]
-	[[Category: Rossello, A]]	+	[[Category: Rossello A]]
-	[[Category: Stura~~, E A~~]]	+	[[Category: Stura EA]]
-	[[Category: Vera, L]]	+	[[Category: Vera L]]
-	~~[[Category: Broad spectrum mmp hydroxamate inhibitor]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Metzincin]]~~	+
-	~~[[Category: Zinc protease~~]]	+

OCA at 16:05, 17 May 2017

OCA — Wed, 17 May 2017 16:05:11 GMT

←Older revision		Revision as of 16:05, 17 May 2017
Line 1:		Line 1:
		+
	==Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor==		==Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor==
	<StructureSection load='4h76' size='340' side='right' caption='[[4h76]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='4h76' size='340' side='right' caption='[[4h76]], [[Resolution\|resolution]] 1.50Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HME, MMP12 ([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">HME, MMP12 ([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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [http://www.ebi.ac.uk/pdbsum/4h76 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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [http://pdbe.org/4h76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [http://www.ebi.ac.uk/pdbsum/4h76 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h76 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4h76" style="background-color:#fffaf0;"></div>

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

OCA at 21:20, 24 December 2014

OCA — Wed, 24 Dec 2014 21:20:57 GMT

←Older revision		Revision as of 21:20, 24 December 2014
Line 9:		Line 9:
	<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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [http://www.ebi.ac.uk/pdbsum/4h76 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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [http://www.ebi.ac.uk/pdbsum/4h76 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 28:
	[[Category: Human]]		[[Category: Human]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]
-	[[Category: Cassar-Lajeunesse, E.]]	+	[[Category: Cassar-Lajeunesse, E]]
-	[[Category: Dive, V.]]	+	[[Category: Dive, V]]
-	[[Category: Nuti, E.]]	+	[[Category: Nuti, E]]
-	[[Category: Rossello, A.]]	+	[[Category: Rossello, A]]
-	[[Category: Stura, E A.]]	+	[[Category: Stura, E A]]
-	[[Category: Vera, L.]]	+	[[Category: Vera, L]]
	[[Category: Broad spectrum mmp hydroxamate inhibitor]]		[[Category: Broad spectrum mmp hydroxamate inhibitor]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]
	[[Category: Metzincin]]		[[Category: Metzincin]]
	[[Category: Zinc protease]]		[[Category: Zinc protease]]

OCA at 05:24, 8 October 2014

OCA — Wed, 08 Oct 2014 05:24:58 GMT

←Older revision		Revision as of 05:24, 8 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4h76\| PDB=4h76 \| SCENE= }}~~	+	==Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor==
-	===Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor===	+	<StructureSection load='4h76' size='340' side='right' caption='[[4h76]], [[Resolution\|resolution]] 1.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23567804}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4h76]] 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=4H76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H76 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=10B:N-2-(BIPHENYL-4-YLSULFONYL)-N-2-(ISOPROPYLOXY)-ACETOHYDROXAMIC+ACID'>10B</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</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">[[4h3x\|4h3x]], [[1rmz\|1rmz]], [[4h30\|4h30]], [[4gr0\|4gr0]], [[4gql\|4gql]], [[3lik\|3lik]], [[3ljg\|3ljg]], [[3lil\|3lil]], [[4efs\|4efs]], [[3tsk\|3tsk]], [[3ts4\|3ts4]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HME, MMP12 ([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='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=4h76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h76 RCSB], [http://www.ebi.ac.uk/pdbsum/4h76 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Homodimerization is important in signal transduction and can play a crucial role in many other biological systems. To obtaining structural information for the design of molecules able to control the signalization pathways, the proteins involved will have to be crystallized in complex with ligands that induce dimerization. Bi-functional drugs have been generated by linking two ligands together chemically and the relative crystallizability of complexes with mono-functional and bi-functional ligands has been evaluated. There are problems associated with crystallization with such ligands, but overall, the advantages appear to be greater than the drawbacks. The study involves two matrix metalloproteinases, MMP-12 and MMP-9. Using flexible and rigid linkers we show that it is possible to control the crystal packing and that by changing the ligand-enzyme stoichiometric ratio, one can toggle between having one bi-functional ligand binding to two enzymes and having the same ligand bound to each enzyme. The nature of linker and its point of attachment on the ligand can be varied to aid crystallization, and such variations can also provide valuable structural information about the interactions made by the linker with the protein. We report here the crystallization and structure determination of seven ligand-dimerized complexes. These results suggest that the use of bi-functional drugs can be extended beyond the realm of protein dimerization to include all drug design projects.

-	~~==Function==~~	+	Crystallization of bi-functional ligand protein complexes.,Antoni C, Vera L, Devel L, Catalani MP, Czarny B, Cassar-Lajeunesse E, Nuti E, Rossello A, Dive V, Stura EA J Struct Biol. 2013 Apr 6. pii: S1047-8477(13)00086-5. doi:, 10.1016/j.jsb.2013.03.015. PMID:23567804<ref>PMID:23567804</ref>
-	~~[[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~~.	+

-	==~~About this Structure~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[~~4h76~~]] ~~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=4H76 OCA].~~	+	</div>
-	[[Category: ~~Homo sapiens~~]]	+
		+	==See Also==
		+	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]
	[[Category: Cassar-Lajeunesse, E.]]		[[Category: Cassar-Lajeunesse, E.]]

OCA at 11:29, 24 April 2013

OCA — Wed, 24 Apr 2013 11:29:04 GMT

←Older revision		Revision as of 11:29, 24 April 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4h76\| PDB=4h76 \| SCENE= }}
		+	===Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor===
		+	{{ABSTRACT_PUBMED_23567804}}

-	~~The entry 4h76 is ON HOLD until Paper Publication~~	+	==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.

-	~~Authors~~: ~~Stura, E~~.A.~~, Vera, L~~., Cassar-Lajeunesse, E., Nuti, E., ~~Dive, V~~., ~~Rossello,~~ A.	+	==About this Structure==
-		+	[[4h76]] 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=4H76 OCA].
-	~~Description~~: ~~Crystal structure of the catalytic domain of Human MMP12 in complex with a broad~~ spectrum hydroxamate inhibitor	+	[[Category: Homo sapiens]]
		+	[[Category: Macrophage elastase]]
		+	[[Category: Cassar-Lajeunesse, E.]]
		+	[[Category: Dive, V.]]
		+	[[Category: Nuti, E.]]
		+	[[Category: Rossello, A.]]
		+	[[Category: Stura, E A.]]
		+	[[Category: Vera, L.]]
		+	[[Category: Broad spectrum mmp hydroxamate inhibitor]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Metzincin]]
		+	[[Category: Zinc protease]]

OCA at 08:37, 31 October 2012

OCA — Wed, 31 Oct 2012 08:37:15 GMT

←Older revision		Revision as of 08:37, 31 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4h76 is ON HOLD	+	The entry 4h76 is ON HOLD until Paper Publication

	Authors: Stura, E.A., Vera, L., Cassar-Lajeunesse, E., Nuti, E., Dive, V., Rossello, A.		Authors: Stura, E.A., Vera, L., Cassar-Lajeunesse, E., Nuti, E., Dive, V., Rossello, A.

	Description: Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor		Description: Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor

OCA: Protected "4h76" [edit=sysop:move=sysop]

OCA — Wed, 26 Sep 2012 20:14:53 GMT

Protected "4h76" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:14, 26 September 2012

OCA: New page: '''Unreleased structure''' The entry 4h76 is ON HOLD Authors: Stura, E.A., Vera, L., Cassar-Lajeunesse, E., Nuti, E., Dive, V., Rossello, A. Description: Crystal structure of the catal...

OCA — Wed, 26 Sep 2012 20:14:52 GMT

New page: '''Unreleased structure''' The entry 4h76 is ON HOLD Authors: Stura, E.A., Vera, L., Cassar-Lajeunesse, E., Nuti, E., Dive, V., Rossello, A. Description: Crystal structure of the catal...

New page

'''Unreleased structure'''

The entry 4h76 is ON HOLD

Authors: Stura, E.A., Vera, L., Cassar-Lajeunesse, E., Nuti, E., Dive, V., Rossello, A.

Description: Crystal structure of the catalytic domain of Human MMP12 in complex with a broad spectrum hydroxamate inhibitor