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2j0t

From Proteopedia

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Current revision (14:31, 13 December 2023) (edit) (undo)
 
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<StructureSection load='2j0t' size='340' side='right'caption='[[2j0t]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
<StructureSection load='2j0t' size='340' side='right'caption='[[2j0t]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2j0t]] is a 6 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=2J0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J0T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2j0t]] 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=2J0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J0T FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ayk|1ayk]], [[1cge|1cge]], [[1cgf|1cgf]], [[1cgl|1cgl]], [[1hfc|1hfc]], [[1su3|1su3]], [[2ayk|2ayk]], [[2clt|2clt]], [[2tcl|2tcl]], [[3ayk|3ayk]], [[4ayk|4ayk]], [[966c|966c]], [[1d2b|1d2b]], [[1lqn|1lqn]], [[1oo9|1oo9]], [[1uea|1uea]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0t OCA], [https://pdbe.org/2j0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j0t RCSB], [https://www.ebi.ac.uk/pdbsum/2j0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j0t 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=2j0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0t OCA], [https://pdbe.org/2j0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j0t RCSB], [https://www.ebi.ac.uk/pdbsum/2j0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j0t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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/TIMP1_HUMAN TIMP1_HUMAN]] Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14.
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[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Interstitial collagenase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Acharya, K R]]
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[[Category: Acharya KR]]
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[[Category: Brew, K]]
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[[Category: Brew K]]
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[[Category: Iyer, S]]
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[[Category: Iyer S]]
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[[Category: Wei, S]]
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[[Category: Wei S]]
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[[Category: Autocatalytic cleavage]]
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[[Category: Collagen degradation]]
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[[Category: Erythrocyte maturation]]
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[[Category: Extracellular matrix]]
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[[Category: Hydrolase]]
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Current revision

Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1

PDB ID 2j0t

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