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==Solution structure of human macrophage elastase (MMP-12) catalytic domain complexed with a gamma-keto butanoic acid inhibitor== | ==Solution structure of human macrophage elastase (MMP-12) catalytic domain complexed with a gamma-keto butanoic acid inhibitor== | ||
<StructureSection load='2z2d' size='340' side='right'caption='[[2z2d | <StructureSection load='2z2d' size='340' side='right'caption='[[2z2d]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2z2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2z2d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z2D 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=HSI:(3R)-3-{4-[(4-CHLOROPHENYL)ETHYNYL]BENZOYL}NONANOIC+ACID'>HSI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=HSI:(3R)-3-{4-[(4-CHLOROPHENYL)ETHYNYL]BENZOYL}NONANOIC+ACID'>HSI</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=2z2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2d OCA], [https://pdbe.org/2z2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z2d RCSB], [https://www.ebi.ac.uk/pdbsum/2z2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z2d 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=2z2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z2d OCA], [https://pdbe.org/2z2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z2d RCSB], [https://www.ebi.ac.uk/pdbsum/2z2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z2d 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. | |||
== 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: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ou L]] | |||
[[Category: Ou | [[Category: Zheng X]] | ||
[[Category: Zheng | |||
Latest revision as of 22:19, 29 May 2024
Solution structure of human macrophage elastase (MMP-12) catalytic domain complexed with a gamma-keto butanoic acid inhibitorSolution structure of human macrophage elastase (MMP-12) catalytic domain complexed with a gamma-keto butanoic acid inhibitor
Structural highlights
FunctionMMP12_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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