Sandbox Reserved 478: Difference between revisions

The Structure of MMP-1 and all other members of the Metalloproteinase family for that matter are formed from three domains. The structure comprises of the N-terminal catalytic domain, the linker region and the C-terminal hemopexin domain. The structure of human MMP-1 was determined with X-Ray Crystallography at a resolution of 2.67A to have two monomers (chains A and B). The catalytic domain of one monomer contacts the hemopexin domain of the other monomer. An interesting observation that has been noted is that the contact site used by the two monomers in the asymmetric unit to form the dimer is not the same as the dimerization site observed in the structure of the MMP-9 hemopexin domain. This difference shows that not all members of the Matrix Metalloproteinase family behave the same in their dimerization processes. Another interesting feature about the protein is that<scene name='Sandbox_Reserved_478/Hydrophobic/1'>Hydrophobic regions</scene> can be found within all areas of the protein rather than being located near a certain domain.  

The <scene name='Sandbox_Reserved_478/Hemopexin/1'>Hemopexin-like Domain</scene> consists of about 210 amino acids and is composed of four Hemopexin modules (I-IV), each representing a blade of the beta-propeller structure. Each blade starts with either the DAA or DAX motif, in which Asp residues direct the central calcium ion through their carbonyl oxygen atom. Glu310 also provides the fourth coordination thus completing the acidic patch at the entrance of the central, solvent-accessible channel. The side chains of these residues also help to form salt bridges with β-strands and hold the entrance of the central channel inline.