Sandbox Reserved 468: Difference between revisions

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'''Catalytic Domain'''
'''Catalytic Domain'''


The Catalytic Domains of all MMPs share very similar characteristics, having the same general shape and 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 shorter 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 the same general shape and 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 <scene name='Sandbox_Reserved_468/Beta_sheets/1'>β-strands</scene>, three <scene name='Sandbox_Reserved_468/Helix/1'>α-helices</scene> 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 shorter form of this domain, where the first 7 amino-acids are not present [6].


Taken from a publication of the crystal structure [3].
Taken from a publication of the crystal structure [3].