Sandbox Reserved 468: Difference between revisions

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Matrix Metalloproteinase-1 (MMP-1)is interstitial collagenase and fibroblast collagenase. The enzyme in humans is encoded by the MMP1 gene. Human Fibroblast Collagenase (MMP-1) was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA.

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 [2].

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.

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 [2].

== Structure ==

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'''Catalytic Domain'''

The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. Despite the similarity of the Catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 Catalytic Domain. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role.

The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. Despite the similarity of the Catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 Catalytic Domain. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role [2].

The Catalytic Domain (CAT) of MMP-1 starts with the F100 as the first amino-acid of the N-terminal loop of the CAT domain. This is different from the first published x-ray structure of the CAT domain was showed the truncated form of this domain, where the first 7 amino-acids are not present.

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== Mechanism of Action ==

There is not very much research that has successfully determined the mechanism of action for this enzyme.

There is not very much research that has successfully determined the mechanism of action for this enzyme but it is known that one zinc ion is at the catalytic site and is responsible for the activity, whereas the other metal ions have structural roles.

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@@ Line 7: / Line 7: @@
 Matrix Metalloproteinase-1 (MMP-1)is interstitial collagenase and fibroblast collagenase. The enzyme in humans is encoded by the MMP1 gene. Human Fibroblast Collagenase (MMP-1) was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA.
-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 [2].
-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.
+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 [2].
 == Structure ==
@@ Line 17: / Line 17: @@
 '''Catalytic Domain'''
-The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. Despite the similarity of the Catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 Catalytic Domain. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role.
+The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. Despite the similarity of the Catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 Catalytic Domain. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role [2].
 The Catalytic Domain (CAT) of MMP-1 starts with the F100 as the first amino-acid of the N-terminal loop of the CAT domain. This is different from the first published x-ray structure of the CAT domain was showed the truncated form of this domain, where the first 7 amino-acids are not present.
@@ Line 38: / Line 38: @@
 == Mechanism of Action ==
-There is not very much research that has successfully determined the mechanism of action for this enzyme.
+There is not very much research that has successfully determined the mechanism of action for this enzyme but it is known that one zinc ion is at the catalytic site and is responsible for the activity, whereas the other metal ions have structural roles.