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| '''Matrix Metalloproteinase 1'''(MMP1) also known as Interstitial collagenase is a zinc-dependent protease that degrades extracellular matrix proteins. Collagenases are enzymes, which cleave bonds in collagen. MMP1 belongs to the Matrix Metalloproteinase (MMP) family, which are involved in the regulation of cell-matrix composition by the breakdown of the extracellular matrix in normal physiological processes. These physiological processes many include disease activities such as arthritis and metastasis as well as normal human reproduction and embryonic development. | | '''Matrix Metalloproteinase 1'''(MMP1) also known as Interstitial collagenase is a zinc-dependent protease that degrades extracellular matrix proteins. Collagenases are enzymes, which cleave bonds in collagen. MMP1 belongs to the Matrix Metalloproteinase (MMP) family, which are involved in the regulation of cell-matrix composition by the breakdown of the extracellular matrix in normal physiological processes. These physiological processes many include disease activities such as arthritis and metastasis as well as normal human reproduction and embryonic development. |
| {{Structure | | {{STRUCTURE_2clt| PDB=2clt | SCENE= }} |
| |PDB= {{{PDB}}}|SCENE={{{SCENE|}}}|SIZE={{{SIZE|350}}}|CAPTION={{{CAPTION|[[2clt]], resolution 2.67Å (<scene name='initialview01'>default scene</scene>)}}} | |
| |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+B'>AC1</scene>
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| |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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| |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] </span>
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| |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00094 HX], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd04278 ZnMc_MMP]</span>
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| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2clt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2clt OCA], [http://www.ebi.ac.uk/pdbsum/2clt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2clt RCSB]</span>
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| |FUNCTION={{GO|id=GO:0008270 | text = zinc ion binding}}{{GO|id=GO:0016787 | text = hydrolase activity}}{{GO|id=GO:0008233 | text = peptidase activity}}{{GO|id=GO:0046872 | text = metal ion binding}}{{GO|id=GO:0003824 | text = catalytic activity}}{{GO|id=GO:0005509 | text = calcium ion binding}}{{GO|id=GO:0008133 | text = collagenase activity}}{{GO|id=GO:0008237 | text = metallopeptidase activity}}{{GO|id=GO:0004232 | text = interstitial collagenase activity}}{{GO|id=GO:0004222 | text = metalloendopeptidase activity}}
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| |PROCESS={{GO|id=GO:0008152 | text = metabolic process}}{{GO|id=GO:0030574 | text = collagen catabolic process}}{{GO|id=GO:0006508 | text = proteolysis}}
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| |COMPONENT={{GO|id=GO:0005578 | text = proteinaceous extracellular matrix}}{{GO|id=GO:0005615 | text = extracellular space}}
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| |SARESOURCES=<span class='plainlinks'>CATH : [http://www.cathdb.info/cgi-bin/cath/Domain.pl?domain_id=2cltA02 2Clta02], [http://www.cathdb.info/cgi-bin/cath/Domain.pl?domain_id=2cltA01 2Clta01], [http://www.cathdb.info/cgi-bin/cath/Domain.pl?domain_id=2cltB01 2Cltb01], [http://www.cathdb.info/cgi-bin/cath/Domain.pl?domain_id=2cltB02 2Cltb02]<br>InterPro : [http://www.ebi.ac.uk/interpro/ISearch?query=IPR002477 Ipr002477], [http://www.ebi.ac.uk/interpro/ISearch?query=IPR001818 Ipr001818], [http://www.ebi.ac.uk/interpro/ISearch?query=IPR006026 Ipr006026], [http://www.ebi.ac.uk/interpro/ISearch?query=IPR000585 Ipr000585], [http://www.ebi.ac.uk/interpro/ISearch?query=IPR006025 Ipr006025]<br>Pfam : [http://pfam.sanger.ac.uk/family?acc=PF00045 PF00045], [http://pfam.sanger.ac.uk/family?acc=PF00413 PF00413]<br>UniProt : [http://ca.expasy.org/cgi-bin/niceprot.pl?P03956 P03956]</span>
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| |FARESOURCES=<span class='plainlinks'>GeneCard : [http://www.genecards.org/cgi-bin/carddisp.pl?id=MMP1 MMP1]</span>
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| |CONSURF={{!}}-
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| {{!}} colspan="2" style="background-color:#bac9f7;color:#040d44;vertical-align:top;text-align:left;" {{!}} [[Image:Consurf_key_small.gif|center]]
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| {{!}}-{{!}} style="background-color:#bac9f7;color:#040d44;vertical-align:top;text-align:left;"
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| {{!}} '''Toggle Conservation Colors:'''
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| {{!}} align="left" style="background-color:#acfaac;border-top:2px solid #dddddd; border-right:2px solid #dddddd" {{!}}
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| Rows = identical sequences:
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| <jmol>
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| <jmolButton>
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| <script></script>
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| <text>A [x]</text>
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| <name>jmb_2clt_A</name>
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| <title>toggle chain A</title>
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| <jsscript>ConsurfChainButton(elementClicked)</jsscript>
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| <appendtargetsuffixtoid>true</appendtargetsuffixtoid>
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| </jmolButton>
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| </jmol>
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| <jmol>
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| <jmolButton>
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| <script></script>
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| <text>B [x]</text>
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| <name>jmb_2clt_B</name>
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| <title>toggle chain B</title>
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| <jsscript>ConsurfChainButton(elementClicked)</jsscript>
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| <appendtargetsuffixtoid>true</appendtargetsuffixtoid>
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| </jmolButton>
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| </jmol>
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| }} | |
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| ==Structure== | | ==Structure== |
| The Structure of MMP-1 and all other members of the Metalloproteinase family for that matter are formed from three domains. The structure comprises of the N-terminal catalytic domain, the linker region and the C-terminal hemopexin domain. The structure of human MMP-1 was determined with X-Ray Crystallography at a resolution of 2.67A to have two monomers (chains A and B). The catalytic domain of one monomer contacts the hemopexin domain of the other monomer. An interesting observation that has been noted is that the contact site used by the two monomers in the asymmetric unit to form the dimer is not the same as the dimerization site observed in the structure of the MMP-9 hemopexin domain. This difference shows that not all members of the Matrix Metalloproteinase family behave the same in their dimerization processes. | | The Structure of MMP-1 and all other members of the Metalloproteinase family for that matter are formed from three domains. The structure comprises of the N-terminal catalytic domain, the linker region and the C-terminal hemopexin domain. The structure of human MMP-1 was determined with X-Ray Crystallography at a resolution of 2.67A to have two monomers (chains A and B). The catalytic domain of one monomer contacts the hemopexin domain of the other monomer. An interesting observation that has been noted is that the contact site used by the two monomers in the asymmetric unit to form the dimer is not the same as the dimerization site observed in the structure of the MMP-9 hemopexin domain. This difference shows that not all members of the Matrix Metalloproteinase family behave the same in their dimerization processes. |