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==Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor== | ==Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor== | ||
<StructureSection load='2k2g' size='340' side='right'caption='[[2k2g | <StructureSection load='2k2g' size='340' side='right'caption='[[2k2g]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k2g]] 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=2K2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2G FirstGlance]. <br> | <table><tr><td colspan='2'>[[2k2g]] 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=2K2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K2G FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSV:N-(DIBENZO[B,D]THIOPHEN-3-YLSULFONYL)-L-VALINE'>DSV</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=2k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2g OCA], [https://pdbe.org/2k2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2g RCSB], [https://www.ebi.ac.uk/pdbsum/2k2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2g 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=2k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2g OCA], [https://pdbe.org/2k2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k2g RCSB], [https://www.ebi.ac.uk/pdbsum/2k2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2g 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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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dwyer B]] | |||
[[Category: Dwyer | [[Category: Li J]] | ||
[[Category: Li | [[Category: Li W]] | ||
[[Category: Li | [[Category: Malakian K]] | ||
[[Category: Malakian | [[Category: Markus MA]] | ||
[[Category: Markus | [[Category: Tsao DHH]] | ||
[[Category: Tsao | [[Category: Wilhelm J]] | ||
[[Category: Wilhelm | [[Category: Wolfrom S]] | ||
[[Category: Wolfrom | |||
Latest revision as of 22:09, 29 May 2024
Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitorSolution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding 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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