Sandbox Reserved 468: Difference between revisions

The structure of human MMP-1 was determined to have two monomeric structures (chains A and B). However, it is believed that this dimer is not physiologically relevant, as it was found that human MMP-1 is a monomer in solution. The structure of MMP-1, just like the other members of matrix metalloproteinases family, is formed by three different domains [2][3]. The structure consists of a <scene name='Sandbox_Reserved_468/Catalytic_domain/3'>Catalytic Domain</scene>, a variable <scene name='Sandbox_Reserved_468/Linker_region/3'>Linker Region</scene> and the <scene name='Sandbox_Reserved_468/Linker_region/1'>Hemopexin-like domain</scene>. The catalytic domain of one monomer is right next to the hemopexin-like domain of the other monomer and is linked by the linker region. Other structural characteristics of MMP-1 include the many <scene name='Sandbox_Reserved_468/Hydrophobic_residues/1'>Hydrophobic residues</scene> found on the protein. 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/organisms.