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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]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''> | <StructureSection load='2k2g' size='340' side='right' caption='[[2k2g]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP12, HME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2g OCA], [http://pdbe.org/2k2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k2g RCSB], [http://www.ebi.ac.uk/pdbsum/2k2g 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=2k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k2g OCA], [http://pdbe.org/2k2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k2g RCSB], [http://www.ebi.ac.uk/pdbsum/2k2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k2g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/2k2g_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/2k2g_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k2g ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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[[Category: Wilhelm, J]] | [[Category: Wilhelm, J]] | ||
[[Category: Wolfrom, S]] | [[Category: Wolfrom, S]] | ||
[[Category: Calcium]] | |||
[[Category: Catalytic domain]] | [[Category: Catalytic domain]] | ||
[[Category: Extracellular matrix]] | [[Category: Extracellular matrix]] | ||
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[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Metalloprotease]] | [[Category: Metalloprotease]] | ||
[[Category: Polymorphism]] | |||
[[Category: Protease]] | [[Category: Protease]] | ||
[[Category: Protein-ligand structure]] | [[Category: Protein-ligand structure]] | ||
[[Category: Secreted]] | [[Category: Secreted]] | ||
[[Category: Zinc]] | |||
[[Category: Zymogen]] | [[Category: Zymogen]] | ||
Revision as of 14:15, 18 July 2018
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
Function[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 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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