Sandbox Reserved 478: Difference between revisions
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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.<ref>Visse</ref> | '''Matrix Metalloproteinase 1'''(MMP1) also known as Interstitial collagenase is a zinc-dependent protease that degrades extracellular matrix proteins. [http://en.wikipedia.org/wiki/Collagenase 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.<ref>Visse</ref> | ||
{{STRUCTURE_2clt| PDB=2clt | SCENE= }} | {{STRUCTURE_2clt| PDB=2clt | SCENE= }} | ||
==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. Another interesting feature about the protein is that<scene name='Sandbox_Reserved_478/Hydrophobic/1'>Hydrophobic regions</scene> can be found within all areas of the protein rather than being located near a certain domain. | 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. Another interesting feature about the protein is that <scene name='Sandbox_Reserved_478/Hydrophobic/1'>Hydrophobic regions</scene> can be found within all areas of the protein rather than being located near a certain domain. | ||
===Catalytic Domain=== | ===Catalytic Domain=== | ||