2wo8: Difference between revisions
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==MMP12 | |||
<StructureSection load='2wo8' size='340' side='right' caption='[[2wo8]], [[Resolution|resolution]] 2.00Å' scene=''> | ==MMP12 complex with a beta hydroxy carboxylic acid== | ||
<StructureSection load='2wo8' size='340' side='right'caption='[[2wo8]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wo8]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2wo8]] is a 4 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=2WO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WO8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=023:N^2^-[(2R)-2-{(1S)-1-[FORMYL(HYDROXY)AMINO]ETHYL}-5-PHENYLPENTANOYL]-N,3-DIMETHYL-L-VALINAMIDE'>023</scene>, <scene name='pdbligand=077:(3S)-5-BIPHENYL-4-YL-3-HYDROXYPENTANOIC+ACID'>077</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=023:N^2^-[(2R)-2-{(1S)-1-[FORMYL(HYDROXY)AMINO]ETHYL}-5-PHENYLPENTANOYL]-N,3-DIMETHYL-L-VALINAMIDE'>023</scene>, <scene name='pdbligand=077:(3S)-5-BIPHENYL-4-YL-3-HYDROXYPENTANOIC+ACID'>077</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2wo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wo8 OCA], [https://pdbe.org/2wo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wo8 RCSB], [https://www.ebi.ac.uk/pdbsum/2wo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wo8 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== 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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/2wo8_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/2wo8_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> | ||
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==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: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Amour | [[Category: Amour AJ]] | ||
[[Category: Baddeley | [[Category: Baddeley SJ]] | ||
[[Category: Brown | [[Category: Brown D]] | ||
[[Category: Convery | [[Category: Convery MA]] | ||
[[Category: Egan | [[Category: Egan D]] | ||
[[Category: Gaines | [[Category: Gaines S]] | ||
[[Category: Gross | [[Category: Gross JW]] | ||
[[Category: Herbert | [[Category: Herbert S]] | ||
[[Category: Holmes | [[Category: Holmes IP]] | ||
[[Category: Lorthioir | [[Category: Lorthioir O]] | ||
[[Category: Martin | [[Category: Martin SL]] | ||
[[Category: Singh | [[Category: Singh OMP]] | ||
[[Category: Smith | [[Category: Smith RH]] | ||
[[Category: Strelow | [[Category: Strelow JM]] | ||
[[Category: Walker | [[Category: Walker A]] | ||
[[Category: Watson | [[Category: Watson SP]] | ||
Latest revision as of 13:15, 9 May 2024
MMP12 complex with a beta hydroxy carboxylic acidMMP12 complex with a beta hydroxy carboxylic acid
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. Publication Abstract from PubMedA new class of selective MMP-12 inhibitors have been identified via high throughput screening. Crystallization with MMP-12 confirmed the mode of binding and allowed initial optimization to be carried out using classical structure based design. The identification of beta-hydroxy carboxylic acids as selective MMP-12 inhibitors.,Holmes IP, Gaines S, Watson SP, Lorthioir O, Walker A, Baddeley SJ, Herbert S, Egan D, Convery MA, Singh OM, Gross JW, Strelow JM, Smith RH, Amour AJ, Brown D, Martin SL Bioorg Med Chem Lett. 2009 Oct 1;19(19):5760-3. Epub 2009 Aug 6. PMID:19703773[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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