1os2: Difference between revisions

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New page: left|200px<br /> <applet load="1os2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1os2, resolution 2.15Å" /> '''Ternary enzyme-prod...
 
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[[Image:1os2.gif|left|200px]]<br />
<applet load="1os2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1os2, resolution 2.15&Aring;" />
'''Ternary enzyme-product-inhibitor complexes of human MMP12'''<br />


==Disease==
==Ternary enzyme-product-inhibitor complexes of human MMP12==
Known diseases associated with this structure: Cardiomyopathy, dilated, 1G OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Cardiomyopathy, familial hypertrophic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Muscular dystrophy, limb-girdle, type 2J OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Myopathy, proximal, with early respiratory muscle involvement OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]], Tibial muscular dystrophy, tardive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188840 188840]]
<StructureSection load='1os2' size='340' side='right'caption='[[1os2]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1os2]] is a 6 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=1OS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OS2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HAE:ACETOHYDROXAMIC+ACID'>HAE</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=1os2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1os2 OCA], [https://pdbe.org/1os2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1os2 RCSB], [https://www.ebi.ac.uk/pdbsum/1os2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1os2 ProSAT]</span></td></tr>
</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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/os/1os2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1os2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1OS2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, CA, ACT, AZI and HAE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OS2 OCA].
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases., Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B, Angew Chem Int Ed Engl. 2003 Jun 16;42(23):2673-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12813751 12813751]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Macrophage elastase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Bertini I]]
[[Category: Bertini, I.]]
[[Category: Calderone V]]
[[Category: Calderone, V.]]
[[Category: Fragai M]]
[[Category: Fragai, M.]]
[[Category: Luchinat C]]
[[Category: Luchinat, C.]]
[[Category: Mangani S]]
[[Category: Mangani, S.]]
[[Category: Terni B]]
[[Category: Terni, B.]]
[[Category: ACT]]
[[Category: AZI]]
[[Category: CA]]
[[Category: HAE]]
[[Category: ZN]]
[[Category: complex (elastase/inhibitor)]]
[[Category: elastase]]
[[Category: hydroxamic acid]]
[[Category: matrix metalloproteinase]]
[[Category: metallo elastase]]
[[Category: mmp12]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:35:57 2007''

Latest revision as of 12:31, 16 August 2023

Ternary enzyme-product-inhibitor complexes of human MMP12Ternary enzyme-product-inhibitor complexes of human MMP12

Structural highlights

1os2 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1os2, resolution 2.15Å

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