Sandbox Reserved 468: Difference between revisions

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== Structure ==

The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by three different subsections. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene>, a variable Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. These structures were determined by using X-ray crystallography and NMR [2][3].

The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by three different subsections. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/3'>Catalytic Domain</scene>, a variable Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. These structures were determined by using X-ray crystallography and NMR [2][3].

Here is the basic structure of a MMP in three different forms.

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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. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands, three α-helix 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 which showed the truncated form of this domain, where the first 7 amino-acids are not present [6].

The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. The <scene name='Sandbox_Reserved_468/Catalytic_domain/3'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands, three α-helix 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 which showed the truncated form of this domain, where the first 7 amino-acids are not present [6].

'''Linker region'''

Sandbox Reserved 468: Difference between revisions

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@@ Line 16: / Line 16: @@
 == Structure ==
-The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by three different subsections. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene>, a variable Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. These structures were determined by using X-ray crystallography and NMR [2][3].
+The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by three different subsections. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/3'>Catalytic Domain</scene>, a variable Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. These structures were determined by using X-ray crystallography and NMR [2][3].
 Here is the basic structure of a MMP in three different forms.
@@ Line 23: / Line 23: @@
 '''Catalytic Domain'''
-The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. The <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands, three α-helix 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 which showed the truncated form of this domain, where the first 7 amino-acids are not present [6].
+The Catalytic Domains of all MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40Å. The <scene name='Sandbox_Reserved_468/Catalytic_domain/3'>Catalytic Domain</scene> of MMP-1 is composed of five highly twisted β-strands, three α-helix 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 which showed the truncated form of this domain, where the first 7 amino-acids are not present [6].
 '''Linker region'''