Sandbox Reserved 468: Difference between revisions
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Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP-1, as with most MMP's, is secreted as inactive proproteins which is later activated when cleaved by extracellular proteases. | Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. MMP-1, as with most MMP's, is secreted as inactive proproteins which is later activated when cleaved by extracellular proteases. | ||
Most MMPs are secreted into the extracellular space as latent enzymes that are activated proteolytically by serine proteinases or by other MMPs. However, one intriguing sub-group of MMPs is the MT-MMPs, membrane-anchored MMPs that are activated intracellularly by a furin-like mechanism and inserted into the membrane in an active form. The first membrane-bound form, MT1-MMP, was described about 10 years ago, and this sub-group now contains six members. Their membrane-bound location appears to confer unique characteristics. Consequently, interest in their structure and function, their pattern of expression and the mechanisms regulating their expression and activity continues to grow. | |||
== Structure == | == Structure == | ||
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A specific region (183)RWTNNFREY(191) as been identified as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. On C-terminal part of the CAT Domain the hB α-helix, known as the "active-site helix" encompasses part of the "zinc-binding consensus sequence" HEXXHXXGXXH that is characteristic of the Metzincin superfamily. The α-helix hB finishes abruptly at Gly225 where the last loop of the domain starts. This last loop contains the "specificity loop" which is the shortest in the MMPs family. The Catalytic Domain ends at Gly261 with α-helix hC. | A specific region (183)RWTNNFREY(191) as been identified as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. On C-terminal part of the CAT Domain the hB α-helix, known as the "active-site helix" encompasses part of the "zinc-binding consensus sequence" HEXXHXXGXXH that is characteristic of the Metzincin superfamily. The α-helix hB finishes abruptly at Gly225 where the last loop of the domain starts. This last loop contains the "specificity loop" which is the shortest in the MMPs family. The Catalytic Domain ends at Gly261 with α-helix hC. | ||
== Mechanism of Action == | |||
There is not very much research that has successfully determined the mechanism of action for this enzyme. | |||
