4h30 - Revision history

OCA at 14:59, 20 September 2023

OCA — Wed, 20 Sep 2023 14:59:07 GMT

←Older revision		Revision as of 14:59, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4h30]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H30 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4h30]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H30 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0ZD:N,N-BIS(2-[(BIPHENYL-4YLSULFONYL)[(2R)-1-HYDROXY-3-METHYL-1-OXOBUTAN-2-YL]-AMINO]ETHYL)BENZENE-1,3-DICARBOXAMIDE'>0ZD</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=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]] 1.43Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0ZD:N,N-BIS(2-[(BIPHENYL-4YLSULFONYL)[(2R)-1-HYDROXY-3-METHYL-1-OXOBUTAN-2-YL]-AMINO]ETHYL)BENZENE-1,3-DICARBOXAMIDE'>0ZD</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=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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [https://pdbe.org/4h30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [https://www.ebi.ac.uk/pdbsum/4h30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h30 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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [https://pdbe.org/4h30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [https://www.ebi.ac.uk/pdbsum/4h30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h30 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:56, 3 November 2022

OCA — Thu, 03 Nov 2022 07:56:59 GMT

←Older revision		Revision as of 07:56, 3 November 2022
Line 1:		Line 1:

	==Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.==		==Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.==
-	<StructureSection load='4h30' size='340' side='right' caption='[[4h30]], [[Resolution\|resolution]] 1.43Å' scene=''>	+	<StructureSection load='4h30' size='340' side='right'caption='[[4h30]], [[Resolution\|resolution]] 1.43Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4h30]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H30 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4H30 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4h30]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H30 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0ZD:N,N-BIS(2-[(BIPHENYL-4YLSULFONYL)[(2R)-1-HYDROXY-3-METHYL-1-OXOBUTAN-2-YL]-AMINO]ETHYL)BENZENE-1,3-DICARBOXAMIDE'>0ZD</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=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=0ZD:N,N-BIS(2-[(BIPHENYL-4YLSULFONYL)[(2R)-1-HYDROXY-3-METHYL-1-OXOBUTAN-2-YL]-AMINO]ETHYL)BENZENE-1,3-DICARBOXAMIDE'>0ZD</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=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4h2e\|4h2e]], [[4h1q\|4h1q]], [[4efs\|4efs]], [[3lir\|3lir]], [[4h3x\|4h3x]]</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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [https://pdbe.org/4h30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [https://www.ebi.ac.uk/pdbsum/4h30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h30 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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [~~http~~://pdbe.org/4h30 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4h30 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4h30 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: Antoni, C]]	+	[[Category: Antoni C]]
-	[[Category: Carafa, L]]	+	[[Category: Carafa L]]
-	[[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: Carboxylic twin inhibitor]]~~	+
-	~~[[Category: Dimerisation]]~~	+
-	~~[[Category: Divalent inhibitor]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibtior complex]]~~	+
-	~~[[Category: Metzincin]]~~	+
-	~~[[Category: Zinc protease~~]]	+

OCA at 16:08, 17 May 2017

OCA — Wed, 17 May 2017 16:08:31 GMT

←Older revision		Revision as of 16:08, 17 May 2017
Line 1:		Line 1:
		+
	==Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.==		==Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.==
	<StructureSection load='4h30' size='340' side='right' caption='[[4h30]], [[Resolution\|resolution]] 1.43Å' scene=''>		<StructureSection load='4h30' size='340' side='right' caption='[[4h30]], [[Resolution\|resolution]] 1.43Å' 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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [http://www.ebi.ac.uk/pdbsum/4h30 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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [http://pdbe.org/4h30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [http://www.ebi.ac.uk/pdbsum/4h30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h30 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 4h30" style="background-color:#fffaf0;"></div>

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

OCA at 20:23, 25 December 2014

OCA — Thu, 25 Dec 2014 20:23:06 GMT

←Older revision		Revision as of 20:23, 25 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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [http://www.ebi.ac.uk/pdbsum/4h30 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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [http://www.ebi.ac.uk/pdbsum/4h30 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: Antoni, C.]]	+	[[Category: Antoni, C]]
-	[[Category: Carafa, L.]]	+	[[Category: Carafa, L]]
-	[[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: Carboxylic twin inhibitor]]		[[Category: Carboxylic twin inhibitor]]
	[[Category: Dimerisation]]		[[Category: Dimerisation]]

OCA at 05:45, 8 October 2014

OCA — Wed, 08 Oct 2014 05:45:27 GMT

←Older revision		Revision as of 05:45, 8 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4h30\| PDB=4h30 \| SCENE= }}~~	+	==Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.==
-	===Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.===	+	<StructureSection load='4h30' size='340' side='right' caption='[[4h30]], [[Resolution\|resolution]] 1.43Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23567804}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4h30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H30 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0ZD:N,N-BIS(2-[(BIPHENYL-4YLSULFONYL)[(2R)-1-HYDROXY-3-METHYL-1-OXOBUTAN-2-YL]-AMINO]ETHYL)BENZENE-1,3-DICARBOXAMIDE'>0ZD</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=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4h2e\|4h2e]], [[4h1q\|4h1q]], [[4efs\|4efs]], [[3lir\|3lir]], [[4h3x\|4h3x]]</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=4h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h30 RCSB], [http://www.ebi.ac.uk/pdbsum/4h30 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>
-	[[~~4h30~~]] ~~is a 2 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H30 OCA].~~	+	</div>
-	[[Category: ~~Homo sapiens~~]]	+
		+	==See Also==
		+	*[[Matrix metalloproteinase\|Matrix metalloproteinase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Macrophage elastase]]		[[Category: Macrophage elastase]]
	[[Category: Antoni, C.]]		[[Category: Antoni, C.]]
Line 21:		Line 37:
	[[Category: Dimerisation]]		[[Category: Dimerisation]]
	[[Category: Divalent inhibitor]]		[[Category: Divalent inhibitor]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
	[[Category: Hydrolase-hydrolase inhibtior complex]]		[[Category: Hydrolase-hydrolase inhibtior complex]]
	[[Category: Metzincin]]		[[Category: Metzincin]]
	[[Category: Zinc protease]]		[[Category: Zinc protease]]

OCA at 11:28, 24 April 2013

OCA — Wed, 24 Apr 2013 11:28:44 GMT

←Older revision		Revision as of 11:28, 24 April 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4h30\| PDB=4h30 \| SCENE= }}
		+	===Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.===
		+	{{ABSTRACT_PUBMED_23567804}}

-	~~The entry 4h30 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~~: ~~Antoni, C~~.~~, Stura, E~~.A.~~, Vera, L~~.~~, Nuti, E~~., Carafa, L., Cassar-Lajeunesse, E., Dive, V., Rossello, A.	+	==About this Structure==
-		+	[[4h30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H30 OCA].
-	~~Description~~: ~~Crystal structure of the catalytic domain of MMP-12 in complex with a~~ twin inhibitor.	+	[[Category: Homo sapiens]]
		+	[[Category: Macrophage elastase]]
		+	[[Category: Antoni, C.]]
		+	[[Category: Carafa, L.]]
		+	[[Category: Cassar-Lajeunesse, E.]]
		+	[[Category: Dive, V.]]
		+	[[Category: Nuti, E.]]
		+	[[Category: Rossello, A.]]
		+	[[Category: Stura, E A.]]
		+	[[Category: Vera, L.]]
		+	[[Category: Carboxylic twin inhibitor]]
		+	[[Category: Dimerisation]]
		+	[[Category: Divalent inhibitor]]
		+	[[Category: Hydrolase-hydrolase inhibtior complex]]
		+	[[Category: Metzincin]]
		+	[[Category: Zinc protease]]

OCA at 20:11, 26 September 2012

OCA — Wed, 26 Sep 2012 20:11:15 GMT

←Older revision		Revision as of 20:11, 26 September 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4h30 is ON HOLD	+	The entry 4h30 is ON HOLD until Paper Publication

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

	Description: Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.		Description: Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.

OCA: Protected "4h30" [edit=sysop:move=sysop]

OCA — Wed, 19 Sep 2012 06:59:04 GMT

Protected "4h30" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:59, 19 September 2012

OCA: New page: '''Unreleased structure''' The entry 4h30 is ON HOLD Authors: Antoni, C., Stura, E.A., Vera, L., Nuti, E., Carafa, L., Cassar-Lajeunesse, E., Dive, V., Rossello, A. Description: Crysta...

OCA — Wed, 19 Sep 2012 06:59:03 GMT

New page: '''Unreleased structure''' The entry 4h30 is ON HOLD Authors: Antoni, C., Stura, E.A., Vera, L., Nuti, E., Carafa, L., Cassar-Lajeunesse, E., Dive, V., Rossello, A. Description: Crysta...

New page

'''Unreleased structure'''

The entry 4h30 is ON HOLD

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

Description: Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.