Sandbox Reserved 1125: Difference between revisions

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It seems that the collagen binds to two sites on MMP-8 : one in the catalytic site and another in the hemopexin domain. One hypothesis is that when the collagen binds to both sites, its helical structure is destabilized and unwound. Thus, the cleavage site of collagen is accessible and the cleavage reaction can occur.[http://www.jleukbio.org/content/81/4/870.full]

Unfortunately, no structure of the full MMP-8 protein has been crystallized yet, but <scene name='71/719866/Human_prommp-1_structure/1'>here</scene> you can see in orange the hemopexin domain of human pro-MMP1 which is very well conserved between these two proteins~~, by the way you can find in~~ this article: [http://www.fasebj.org/content/12/12/1075.full#ref-27 Matrix metalloproteinases: structures, evolution, and diversification,Irina Massova, Lakshmi P. Kotra, Rafael Fridman and Shahriar Mobashery], good pieces of information on conservations among the MMPs family.

Unfortunately, no structure of the full MMP-8 protein has been crystallized yet, but <scene name='71/719866/Human_prommp-1_structure/1'>here</scene> you can see in orange the hemopexin domain of human pro-MMP1 which is very well conserved between these two proteins. In this article [http://www.fasebj.org/content/12/12/1075.full#ref-27 Matrix metalloproteinases: structures, evolution, and diversification,Irina Massova, Lakshmi P. Kotra, Rafael Fridman and Shahriar Mobashery], there are good pieces of information on conservations among the MMPs family.

Sandbox Reserved 1125: Difference between revisions

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Revision as of 18:15, 30 January 2016 view source Laura Dutto (talk \| contribs) 167 edits No edit summary ← Older edit		Revision as of 18:18, 30 January 2016 view source Laura Dutto (talk \| contribs) 167 edits No edit summary Newer edit →
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	It seems that the collagen binds to two sites on MMP-8 : one in the catalytic site and another in the hemopexin domain. One hypothesis is that when the collagen binds to both sites, its helical structure is destabilized and unwound. Thus, the cleavage site of collagen is accessible and the cleavage reaction can occur.[http://www.jleukbio.org/content/81/4/870.full]		It seems that the collagen binds to two sites on MMP-8 : one in the catalytic site and another in the hemopexin domain. One hypothesis is that when the collagen binds to both sites, its helical structure is destabilized and unwound. Thus, the cleavage site of collagen is accessible and the cleavage reaction can occur.[http://www.jleukbio.org/content/81/4/870.full]

	Unfortunately, no structure of the full MMP-8 protein has been crystallized yet, but <scene name='71/719866/Human_prommp-1_structure/1'>here</scene> you can see in orange the hemopexin domain of human pro-MMP1 which is very well conserved between these two proteins~~, by the way you can find in~~ this article: [http://www.fasebj.org/content/12/12/1075.full#ref-27 Matrix metalloproteinases: structures, evolution, and diversification,Irina Massova, Lakshmi P. Kotra, Rafael Fridman and Shahriar Mobashery], good pieces of information on conservations among the MMPs family.		Unfortunately, no structure of the full MMP-8 protein has been crystallized yet, but <scene name='71/719866/Human_prommp-1_structure/1'>here</scene> you can see in orange the hemopexin domain of human pro-MMP1 which is very well conserved between these two proteins. In this article [http://www.fasebj.org/content/12/12/1075.full#ref-27 Matrix metalloproteinases: structures, evolution, and diversification,Irina Massova, Lakshmi P. Kotra, Rafael Fridman and Shahriar Mobashery], there are good pieces of information on conservations among the MMPs family.