Sandbox Reserved 468: Difference between revisions
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== Structure == | == Structure == | ||
The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by different subsections. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/2'>Catalytic Domain</scene>, a Linker Region and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. | 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]. | ||
Here is the basic structure of a MMP in three different forms. | Here is the basic structure of a MMP in three different forms. | ||
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'''Catalytic Domain''' | '''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 | 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]. | ||
'''Linker region''' | '''Linker region''' | ||
In MMPs the catalytic domain is followed by a stretch of 15–65 amino acid residues referred to as the linker or the hinge region. This region is rich in proline residues | In MMPs the catalytic domain is followed by a stretch of 15–65 amino acid residues referred to as the linker or the hinge region. The length of this region varies between MMPs and does not have a well-determined structure. This region is typically rich in proline residues. Interestingly, the replacement of those with alanine drastically reduced the collagenolytic activity of certain MMPs, which may indicate that the presence of the correct linker structure is important for collagenolysis [4]. | ||
'''Hemopexin-like domain''' | '''Hemopexin-like domain''' | ||
