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<StructureSection load='1cgl' size='340' side='right'caption='[[1cgl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1cgl' size='340' side='right'caption='[[1cgl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cgl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CGL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cgl]] is a 2 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=1CGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CGL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0ED:N-[(1S)-3-{[(BENZYLOXY)CARBONYL]AMINO}-1-CARBOXYPROPYL]-L-LEUCYL-N-(2-MORPHOLIN-4-YLETHYL)-L-PHENYLALANINAMIDE'>0ED</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0ED:N-[(1S)-3-{[(BENZYLOXY)CARBONYL]AMINO}-1-CARBOXYPROPYL]-L-LEUCYL-N-(2-MORPHOLIN-4-YLETHYL)-L-PHENYLALANINAMIDE'>0ED</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1cgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgl OCA], [https://pdbe.org/1cgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cgl RCSB], [https://www.ebi.ac.uk/pdbsum/1cgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cgl 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=1cgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgl OCA], [https://pdbe.org/1cgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cgl RCSB], [https://www.ebi.ac.uk/pdbsum/1cgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cgl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MMP1_HUMAN MMP1_HUMAN]] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.<ref>PMID:1645757</ref>
[https://www.uniprot.org/uniprot/MMP1_HUMAN MMP1_HUMAN] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.<ref>PMID:1645757</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1cgl ConSurf].
</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=1cgl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Collagenase is a zinc-dependent endoproteinase and is a member of the matrix metalloproteinase (MMP) family of enzymes. The MMPs participate in connective tissue remodeling events and aberrant regulation has been associated with several pathologies. The 2.4 angstrom resolution structure of the inhibited enzyme revealed that, in addition to the catalytic zinc, there is a second zinc ion and a calcium ion which play a major role in stabilizing the tertiary structure of collagenase. Despite scant sequence homology, collagenase shares structural homology with two other endoproteinases, bacterial thermolysin and crayfish astacin. The detailed description of protein-inhibitor interactions present in the structure will aid in the design of compounds that selectively inhibit individual members of the MMP family. Such inhibitors will be useful in examining the function of MMPs in pathological processes.
Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor.,Lovejoy B, Cleasby A, Hassell AM, Longley K, Luther MA, Weigl D, McGeehan G, McElroy AB, Drewry D, Lambert MH, et al. Science. 1994 Jan 21;263(5145):375-7. PMID:8278810<ref>PMID:8278810</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1cgl" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Interstitial collagenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cleasby, A]]
[[Category: Cleasby A]]
[[Category: Drewry, D]]
[[Category: Drewry D]]
[[Category: Hassell, A M]]
[[Category: Hassell AM]]
[[Category: Jordan, S R]]
[[Category: Jordan SR]]
[[Category: Lambert, M H]]
[[Category: Lambert MH]]
[[Category: Longley, K]]
[[Category: Longley K]]
[[Category: Lovejoy, B]]
[[Category: Lovejoy B]]
[[Category: Luther, M A]]
[[Category: Luther MA]]
[[Category: Mcelroy, A B]]
[[Category: Mcelroy AB]]
[[Category: Mcgeehan, G]]
[[Category: Mcgeehan G]]
[[Category: Weigl, D]]
[[Category: Weigl D]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Metalloprotease]]

Latest revision as of 06:42, 7 February 2024

Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor

1cgl, resolution 2.40Å

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